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(A)15 + n ATP
(A)15+n + n diphosphate
in the presence of ATP, the incorporation of several nucleotides into the RNA substrate is observed
-
-
?
(A)n + ATP
(A)n+1 + diphosphate
-
-
-
?
(A)n + CTP
(A)n-C + diphosphate
-
-
-
?
(A)n + diphosphate
(A)n-1 + ATP
-
-
-
?
(A)n + GTP
(A)n-G + diphosphate
-
-
-
?
2-aminopurine riboside triphosphate + RNA
?
-
-
-
?
adenosine 5'-O-(1-thiotriphosphate) + RNA
diphosphate + ?
-
SP-diastereomer
-
-
?
ATP + 3' untranslated region of mRNA
diphosphate + ?
-
-
-
?
ATP + adenosine(5')diphospho(5')adenosine
diphosphate + ?
-
i.e. AP2A
-
-
?
ATP + adenosine(5')pentaphospho(5')adenosine
diphosphate + ?
-
i.e. AP5A
-
-
?
ATP + adenosine(5')tetraphospho(5')adenosine
diphosphate + ?
-
i.e. AP4A
-
-
?
ATP + adenosine(5')triphospho(5')adenosine
diphosphate + ?
-
i.e. AP3A
-
-
?
ATP + AMP
diphosphate + ?
-
-
-
-
?
ATP + CMP
diphosphate + ?
-
-
-
-
?
ATP + CTP
diphosphate + ?
-
-
-
-
?
ATP + dGTP
diphosphate + ?
-
-
-
-
?
ATP + GDP
diphosphate + ?
-
-
-
-
?
ATP + GLUT1 mRNA poly(A) tail
?
-
-
-
?
ATP + GTP
diphosphate + ?
-
-
-
-
?
ATP + guanosine
diphosphate + ?
-
-
-
-
?
ATP + guanosine(5')diphospho(5')guanosine
diphosphate + ?
-
i.e. GP2G
-
-
?
ATP + guanosine(5')pentaphospho(5')guanosine
diphosphate + ?
-
i.e. GP5G
-
-
?
ATP + guanosine(5')tetraphospho(5')guanosine
diphosphate + ?
-
i.e. GP4G
-
-
?
ATP + guanosine(5')triphospho(5')guanosine
diphosphate + ?
-
i.e. GP3G
-
-
?
ATP + IMP
diphosphate + ?
-
-
-
-
?
ATP + miR-21-5p
?
enzyme isoform PAPD5 adenylates the 3'-end of miR-21-5p, marking it for 3'-to-5'-trimming by the poly(A) specific ribonuclease PARN
-
-
?
ATP + myosin short poly(A)
?
-
-
-
-
?
ATP + nucleotide
?
-
-
-
-
?
ATP + oligo(A)12
diphosphate + oligo(A)13
ATP + oligo(A)14
diphosphate + oligo(A)15
-
-
-
-
?
ATP + oligo(A)15
diphosphate + oligo(A)16
ATP + oligo(A)17C
diphosphate + oligo(A)18C
-
-
-
-
?
ATP + oligo(A)18
diphosphate + oligo(A)19
ATP + oligo(A)n
diphosphate + oligo(A)n+1
ATP + oligo(U)n
diphosphate + ?
-
-
-
?
ATP + oligoadenylate
?
-
-
-
-
?
ATP + poly(A)n
diphosphate + poly(A)n+1
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
ATP + RNA (A)15
diphosphate + RNA (A)16
-
-
-
-
?
ATP + RNA (A)15
diphosphate + RNA(A)16
ATP + RNA primer
?
-
-
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
ATP + RNA(A)15
diphosphate + RNA(A)16
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
ATP + rRNA
diphosphate + ?
-
-
-
?
ATP + XTP
diphosphate + ?
-
-
-
-
?
ATP + yeast tRNAiMet
diphosphate + ?
in vitro-synthesized yeast tRNAiMet, but not the native tRNA is substrate
-
-
?
CTP + RNA
diphosphate + ?
-
12% of the activity with ATP, adenylyltransferase A
-
-
?
CTP + RNA primer
diphosphate + RNA primer-C
enzyme can use UTP, CTP and GTP as co-substrates in vitro
enzyme can use UTP, CTP and GTP as co-substrates in vitro
-
?
CTP + RNAn
diphosphate + RNAn+1
dATP + RNA
diphosphate + ?
-
15% of the activity with ATP
-
-
?
GTP + RNA primer
diphosphate + RNA primer-G
-
enzyme can use UTP, CTP and GTP as co-substrates in vitro
-
?
mRNA of isoform gld-1 + ATP
polyadenylated mRNA of isoform gld-1 + diphosphate
-
reaction catalyzed by enzyme isoform GLD-2
-
-
?
UTP + RNA
diphosphate + RNA(U)n
-
recombinant Cid1 shows a preference for UTP over ATP, the poly(U) polymerase activity of recombinant Cid1 out-competes its PAP activity under physiologically relevant conditions
-
-
?
UTP + RNA primer
diphosphate + RNA primer-U
-
enzyme can use UTP, CTP and GTP as co-substrates in vitro
-
?
additional information
?
-
ATP + oligo(A)12
diphosphate + oligo(A)13
-
-
-
-
?
ATP + oligo(A)12
diphosphate + oligo(A)13
-
-
-
?
ATP + oligo(A)15
diphosphate + oligo(A)16
-
-
-
?
ATP + oligo(A)15
diphosphate + oligo(A)16
-
-
-
?
ATP + oligo(A)18
diphosphate + oligo(A)19
-
-
-
?
ATP + oligo(A)18
diphosphate + oligo(A)19
-
-
-
-
?
ATP + oligo(A)n
diphosphate + oligo(A)n+1
-
-
-
-
?
ATP + oligo(A)n
diphosphate + oligo(A)n+1
-
-
-
?
ATP + RNA
?
-
processing and activation of stored mRNAs after resumption of development
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA
?
Coturnix sp.
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
the enzymatic machinery that catalyzes formation of 3'-ends of polyadenylated mRNAs consists of two distinct factors: a poly(A) polymerase and a cleavage/specificity factor required for the correct cleavage at the poly(A) site of pre-mRNA
-
-
?
ATP + RNA
?
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
synthetic and hydrolytic activities are functions of the same molecule, the level of adenine nucleotides regulates synthesis and degradation of poly(A), the hydrolytic reaction is responsible for poly(A) shortening or turnover, poly(A) itself is a storage form of adenine nucleotides
-
-
?
ATP + RNA
?
-
2 enzymes participate in the polyadenylation of chromosomal RNA, by a coupled mechanism, the chromatin bound enzyme adds 120-130 adenosine nucleotides to chromosomal RNA, the nucleoplasmic enzyme completes the polyadenylation by adding 80-90 more AMP units to the polyadenylated end
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
length of the poly(A) tail is dependent on incubation time and RNA primer concentration
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
length of the poly(A) tail is dependent on incubation time and RNA primer concentration
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme also has cleavage activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(A)
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: dephosphorylated poly(A), tRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
elongation of the primer is distributive
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: viral RNA MS-2 and QB
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: short poly(U)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated enzyme from calf thymus or HeLa cells prefers either longer poly(A) or RNAs rather than shorter oligomers of AMP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
polyadenylate sequences of 100-200 AMP residues
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme has no ATPase or poly(A) degrading activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(G,U)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides when poly(C) and poly(I), but not poly(U), primes poly(A) synthesis with the Mg2+-activated enzyme
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: rRNA 16S, E. coli
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: rRNA 23S, E. coli
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: phage RNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
poly(A) is the most effective primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
influence of shape and size on priming efficiency
polyadenylate sequences of 100-200 AMP residues
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated calf thymus enzyme uses poly(A), tRNA, small RNA fragments from calf thymus RNA well, but HeLa 18 and 28S rRNA and MS-1 RNA poorly if at all
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: variety of oligoribonucleotides having free 3'-OH
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(G)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(C)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
adenosine 5'-(beta,gamma-methylene)triphosphate is efficiently polymerized into poly(A) with a polymerase from quail oviduct
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primers: poly(U), poly(C), poly(A), not poly(G)
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme uses all four nucleoside triphosphates
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme is unable to catalyze pyrophosphorolysis or phosphorolysis reaction
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
highly specific for ATP
-
-
r
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated enzyme from calf thymus or HeLa cells prefers either longer poly(A) or RNAs rather than shorter oligomers of AMP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme also has cleavage activity
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
human nuclear enzyme and Vaccinia virus enzyme are able to use both RNA and oligo(A) as primer, human cytoplasmic enzyme is able to use RNA but not oligo(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated calf thymus enzyme uses poly(A), tRNA, small RNA fragments from calf thymus RNA well, but HeLa 18 and 28S rRNA and MS-1 RNA poorly if at all
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Hs2 complexes have very little PAP activity, Hs2 also displays efficient poly(U) polymerase activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
-
polymerase IIa and IIb utilize a variety of natural and synthetic RNAs as well as DNA as primer
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
poly(A) and poly(C) minimally effective
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(dT)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: oligonucleotides A-A-A-A and A-A-A
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(U)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
chromatin enzyme uses chromosomal RNA as primer, enzyme from nucleoplasm uses poly(A) and hnRNA isolated from chromatin as primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
-
primer required
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
catalyzes the synthesis of polyadenylate linked to the 3'-hydroxyl end of the terminal nucleoside of an RNA primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: tRNA lacking terminal adenosine
-
?
ATP + RNA
diphosphate + RNA(A)n
-
ATP is utilized 2000-fold more than any other nucleoside triphosphate tested
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme also catalyzes hydrolysis of poly(A)
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
-
does not degrade poly(A) associated with poly(A)*poly(U) helical structure
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
-
poly(A) is the most effective primer
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
mitochondrial RNA at least five times more efficiently used than nuclear RNA
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: methionyl-tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: various E. coli tRNAs or rRNAs
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
elongation of the primer is distributive
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: RNA homopolymers
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
PAP catalyzes the synthesis of poly(A) tails on the 3'-end of pre-mRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
human nuclear enzyme and Vaccinia virus enzyme are able to use both RNA and oligo(A) as primer, human cytoplasmic enzyme is able to use RNA but not oligo(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
minimum effective primer length is 4 to 6 nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: dinucleoside phosphates having 3'-OH
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
catalyzes the synthesis of polyadenylate linked to the 3'-hydroxyl end of the terminal nucleoside of an RNA primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: tRNA lacking terminal adenosine
-
?
ATP + RNA
diphosphate + RNA(A)n
-
ATP is utilized 2000-fold more than any other nucleoside triphosphate tested
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: methionyl-tRNA
-
?
ATP + RNA (A)15
diphosphate + RNA(A)16
-
-
-
?
ATP + RNA (A)15
diphosphate + RNA(A)16
-
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
in absence of ATP: no activity with 8-Cl-ATP, and 8-amino-ATP results in chain termination, in presence of ATP: polyadenylation of the primer is blocked (inhibited) by 8-amino-ATP and 8-Cl-ATP
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
isoform GLD-2 shows specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
-
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
-
isoform PAPD7 displays strong nucleotidyl transferase activity
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
in the assay ATP is added to a final concentration of 0.25 mM
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
adenine can bind in two different configurations in the PAP active site
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
preferentially elongates RNA harbouring poly(A) tails bound by Hfq
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
additional information
?
-
in Aquifex aeolicus, 3'-terminal CCA (CCA-3' at positions 7476) of tRNA is synthesized by CC-adding and A-adding enzymes collaboratively. CC addition onto tRNA is catalyzed by poly A polymerase. After C74 addition in an enclosed active pocket and diphosphate release, the tRNA translocates and rotates relative to the enzyme, and C75 addition occurs in the same active pocket as C74 addition. At both the C74-adding and C75-adding stages, CTP is selected by Watson-Crick-like hydrogen bonds between the cytosine of CTP and conserved Asp and Arg residues in the pocket. After C74C75 addition and diosphate release, the tRNA translocates further and drops off the enzyme
-
-
?
additional information
?
-
-
in Aquifex aeolicus, 3'-terminal CCA (CCA-3' at positions 7476) of tRNA is synthesized by CC-adding and A-adding enzymes collaboratively. CC addition onto tRNA is catalyzed by poly A polymerase. After C74 addition in an enclosed active pocket and diphosphate release, the tRNA translocates and rotates relative to the enzyme, and C75 addition occurs in the same active pocket as C74 addition. At both the C74-adding and C75-adding stages, CTP is selected by Watson-Crick-like hydrogen bonds between the cytosine of CTP and conserved Asp and Arg residues in the pocket. After C74C75 addition and diosphate release, the tRNA translocates further and drops off the enzyme
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
enzyme isoform GLD-2 enhances entry into the meiotic cell cycle at least in part by activating oisoform GLD-1 expression
-
-
?
additional information
?
-
-
dATP is not used efficiently by the PAP protein, neither CTP nor UTP is an effective substrate, GTP is used at 6.3% of the rate of ATP
-
-
?
additional information
?
-
Coturnix sp.
-
overview on substrates and primers
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
rRNA fragments and tRNA precursors originating from the internal spacer regions of the rrn operons, in particular, rrnB are abundant poly(A) polymerase targets. Glu tRNA precursors originating from the rrnB and rrnG transcripts exhibit long 3' trailers that are primarily removed by polyribonucleotide nucleotidyltransferase and to a lesser extent by RNase II and poly(A) polymerase. Glu tRNA precursors still harbouring the 5' leader can be degraded by a 3' to 5' quality control pathway involving poly(A) polymerase
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
the enzyme is responsible for the synthesis of the poly(A) tail at the 3'-end of eukaryotic mRNA
-
-
?
additional information
?
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
?
additional information
?
-
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
?
additional information
?
-
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
?
additional information
?
-
-
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
enzyme may act in the ooplasm on the progression of metaphase I to metaphase II during oocyte maturation
-
-
?
additional information
?
-
-
PAP is a substrate for extracellular signal-regulated kinase
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
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NH4+
-
maximal activity at 33 mM, inhibition above 150 mM
KCl
-
requirement is dependent on the primer and the divalent cation used
KCl
-
maximal stimulation at 40 mM, inhibition above 250 mM
KCl
-
maximal activity at 33 mM, inhibition above 150 mM
KCl
-
optimal concentration: 60 mM
Mg2+
more active in presence of Mg2+ than Mn2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
optimal concentration is about 5 mM
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
optimal concentration: 4-6 mM
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
completely inactive in presence of Mg2+
Mg2+
-
one-fifth of the activity of Mg2+ in NTP activation
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
Coturnix sp.
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA
Mg2+
-
optimal concentration: 5 mM
Mg2+
-
Mg2+ or Mn2+ required
Mg2+
-
NE PAP I (isoenzyme from cytoplasmic fraction) and S100 PAP (isoenzyme from nuclear fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mg2+
-
in presence of Mg2+ and a specificity factor required for correct cleavage at the poly(A) site of pre-mRNA
Mg2+
-
Mg2+ ions can release the inhibition of PAPgamma by aminoglycosides
Mg2+
0.5 mM used in assay conditions
Mg2+
4 mM used in assay conditions. When Mg2+ is replaced by Mn2+, the protein becomes more potent in catalyzing polyadenylation
Mg2+
-
Mg2+ is inactive, maximum activity in presence of both Mn2+ and Mg2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
0.5 mM used in assay conditions
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
more active in presence of Mg2+ than Mn2+
Mg2+
-
10% of the activity with Mn2+
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
optimal concentration: 8-10 mM, polymerase I from chromatin, polymerase II from nucleoplasm is inactive in presence of Mg2+
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
essential for activity
Mg2+
required for activity
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
optimal concentration depends on ATP concentration
Mg2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mg2+
-
more active in presence of Mn2+ than Mg2+
Mg2+
-
Vaccinia virus enzyme is stimulated by Mn2+ and also by Mg2+
Mg2+
4 mM used in assay conditions. When Mg2+ is replaced by Mn2+, the protein becomes more potent in catalyzing polyadenylation
Mg2+
-
ATP is utilized 150-fold more with Mn2+ than with Mg2+
Mn2+
more active in presence of Mg2+ than Mn2+
Mn2+
-
exclusively activated by Mn2+
Mn2+
-
optimal concentration: 2-4 mM
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
more active in presence of Mg2+ than Mn2+
Mn2+
-
optimal concentration: 0.5 mM (at 0.5 mM ATP)
Mn2+
-
required for NTP activation
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
Coturnix sp.
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
optimal concentration: 2 mM
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
HeLa cells contain one enzyme form that is stimulated by Mn2+ and also by Mg2+, and a second one that is absolutely dependent on the presence of Mg2+
Mn2+
-
NE PAP I (isoenzyme from nuclear fraction) and S100 PAP (isoenzyme from cytoplasmic fraction): higher activity in presence of Mn2+ than in presence of Mg2+, NE PAP II: approximately equal levels in presence of Mn2+ and Mg2+
Mn2+
-
nonspecific adenylation of RNA in presence of Mn2+
Mn2+
0.5 mM used in assay conditions
Mn2+
4 mM used in assay conditions
Mn2+
-
maximum activity in presence of both Mn2+ and Mg2+
Mn2+
-
optimal concentration: 4 mM (polymerase IIa), 4-8 mM (polymerase IIb)
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
0.5 mM used in assay conditions
Mn2+
0.5 mM used in assay conditions
Mn2+
-
more active in presence of Mg2+ than Mn2+
Mn2+
-
absolute requirement
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
optimal concentration: 0.50-0.75 mM
Mn2+
-
optimal concentration: 0.25-1.0 mM
Mn2+
-
optimal concentration: 0.8 mM (polymerase I and II)
Mn2+
-
optimal concentration: 0.25-0.75 mM
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
optimal concentration depends on ATP concentration
Mn2+
-
Mg2+ can partially replace Mn2+ in the reaction with polymerase II
Mn2+
-
divalent cation requirement may be fulfilled by Mn2+, Mg2+ or a combination of the two depending on the source of the enzyme
Mn2+
-
more active in presence of Mn2+ than Mg2+
Mn2+
-
Vaccinia virus enzyme is stimulated by Mn2+ and also by Mg2+
Mn2+
-
optimal concentration: 2 mM
Mn2+
4 mM used in assay conditions
Mn2+
-
ATP is utilized 150-fold more with Mn2+ than with Mg2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
Coturnix sp.
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
additional information
-
low ionic strength required for maximal activity
additional information
-
overview: ion requirements, poly(A) polymerases purified from different sources, and in some cases even from the same source, respond differently to the presence of Mg2+ and Mn2+
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3'-Acetyl-1'-benzyl-2'-methylpyrrolo[3,2-C]4-deoxyrifamycin
-
-
3-(4-Benzyl-2,6-dimethyl piperazinoiminomethyl)rifamycin SV
-
-
3-(4-Ethylpiperazinoiminomethyl) rifamycin SV
-
-
5-epi-sisomycin
-
pH-dependent inhibition, non-competitive inhibitor for ATP
8-amino-ATP
-
C-8 substitution influences sugar pucker conformation, which may affect yPAP efficiently
8-aza-ATP
-
slight inhibition
8-azido-ATP
-
slight inhibition
8-bromo-ATP
-
halogen modification at C-8 may negatively affect the ability of the enzyme to activate the ATP substrate or to transfer the AMP group from the enzyme to the RNA substrate
adenosine 5'-(alpha,beta-methylenetriphosphate)
-
-
adenylyl-(3'-5')adenosine
-
-
Adenylyl-(3'-5')cytosine
-
-
ADP
-
inhibits hydrolytic reaction
alpha, beta-methylene-ATP
-
a nonreactive ATP analogue
AMP
-
inhibits hydrolytic reaction
aurintricarboxylic acid
-
-
CaCl2
-
remaining activity 3%
CoCl2
-
remaining activity 75%
Cordycepin 5'-triphosphate
-
-
Cordycepin triphosphate
-
5.0 mM
CuCl2
-
remaining activity 0.1%
EDTA
100% inhibition at 0.5 mM
GMP
-
1 mM, complete inhibition of enzymic reaction with tRNA
hygromycin B
-
pH-dependent inhibition
kanamycin A
-
pH-dependent inhibition
kanamycin B
-
pH-dependent inhibition
KCl
-
stimulation at low concentrations, at 300 mM, 15% inhibition, major poly(A) polymerase, 52% inhibition, minor poly(A) polymerase
lividomycin A
-
pH-dependent inhibition
Mn2+
-
high concentrations
NaF
-
10 mM, complete inhibition
neomycin B
-
an increase in pH releases the neomycin B inhibitory effect on PAPgamma
Pancreatic ribonuclease
-
-
-
paromomycin
-
pH-dependent inhibition
PD98059
-
induces partial inhibition of PAP phosphorylation at S537
Ribonucleoside triphosphates other than ATP
-
-
ribostamycin
-
pH-dependent inhibition
Rifamycin B:N,N-diethylamide
-
-
Rifamycin B:N,N-dipentylamide
-
-
Rifamycin derivatives
-
some derivatives are effective, others not
-
sisomicin
-
pH-dependent inhibition, non-competitive inhibitor for ATP
small ubiquitin-like modifier
-
in vitro sumoylation inhibits the activity of purified PAP
-
tobramycin
-
pH-dependent inhibition
1,10-phenanthroline
-
1 mM, 28% inhibition, major poly(A) polymerase, 50% inhibition, minor poly(A) polymerase
2'-dATP
-
-
3'-dATP
-
-
ATP
-
above 0.5 mM
ATP
-
hepatoma enzyme less effective to substrate inhibition than liver enzyme
ATP
-
inhibits hydrolytic reaction
cordycepin
-
not
CTP
-
-
dATP
-
dATP
-
0.25 mM, 50% inhibition, major poly(A) polymerase, 15% inhibition, minor poly(A) polymerase
diphosphate
-
noncompetitive to ATP and primer
diphosphate
Coturnix sp.
-
noncompetitive to ATP and primer
diphosphate
-
noncompetitive to ATP and primer
diphosphate
-
noncompetitive to ATP and primer
diphosphate
-
noncompetitive to ATP and primer
diphosphate
-
noncompetitive to ATP and primer
diphosphate
-
noncompetitive to ATP and primer
diphosphate
-
product inhibitor
diphosphate
-
noncompetitive to ATP and primer
GTP
-
K+
-
-
K+
-
80 mM: 50% inhibition; KCl
K+
Coturnix sp.
-
above 50 mM; KCl
K+
-
KCl; maximal stimulation at 40 mM, inhibition above 250 mM
N-ethylmaleimide
-
inhibits Mn2+-activated enzyme
N-ethylmaleimide
-
inhibits Mn2+-activated enzyme
Na+
-
-
Na+
Coturnix sp.
-
above 50 mM; NaCl
Na2HPO4
-
-
Na2HPO4
-
dibasic sodium phosphate
NH4+
-
-
NH4+
-
50 mM: 50% inhibition; ammonium sulfate
NH4+
-
10-40 mM; ammonium sulfate
NH4+
-
ammonium sulfate; maximal activity at 33 mM, inhibition above 150 mM
NH4+
-
0.1 M polymerase Ia and Ib completely inhibited, polymerase II: 68% inhibition; ammonium sulfate
phosphate
-
-
phosphate
-
not: rat liver nuclear enzyme
PO43-
-
not inhibitory
Poly(dT)
-
-
polyamines
-
-
-
polyamines
Coturnix sp.
-
-
-
Polyphosphate
-
with 20 nM to 0.002 mM of polyphosphate the length of the products is reduced but inhibition is not complete
Polyphosphate
-
inhibition depends on chain length, P3 10% at 0.001 mM, P4 60% at 0.001 mM, P15 90% at 0.001 mM, P35 100% at 0.001 mM
Polyphosphate
-
potent inhibitor of poly(A) polymerase activity, almost complete inhibition at 200 nM
Proflavine
-
only at very high levels
Proflavine
Coturnix sp.
-
only at very high levels
Proflavine
-
only at very high levels
Proflavine
-
only at very high levels
Proflavine
-
only at very high levels
Proflavine
-
only at very high levels
Proflavine
-
only at very high levels
Proflavine
-
only at very high levels
rifampicin
-
not inhibitory
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
Coturnix sp.
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
rifamycin AF/013
-
O-n-octyloxime of 3-formylrifamycin SV
SO42-
-
-
spermine
-
inhibition if poly(A), nuclear RNA, or tRNA serves as primer, not with short oligonucleotide primers such as (Ap)3A
spermine
-
inhibition if poly(A), nuclear RNA, or tRNA serves as primer, not with short oligonucleotide primers such as (Ap)3A
UTP
-
-
Zn2+
-
-
Zn2+
-
inhibits PAP activity at concentrations above 10 µM in the presence of 5 mM MgCl2
additional information
-
not inhibitory: rifampicin, streptolydigin, phosphate at 0.5 mM, cordycepin at 0.1 mM
-
additional information
-
overview
-
additional information
-
not inhibitory: actinomycin D; not inhibitory: alpha-amanitin
-
additional information
-
insensitive to high levels of RNA-polymerase inhibitors
-
additional information
Coturnix sp.
-
overview
-
additional information
-
overview
-
additional information
-
overview
-
additional information
-
stem-loop structure in mRNA 3-ends may be inhibitory
-
additional information
-
overview
-
additional information
-
not inhibited by neamine
-
additional information
-
not inhibitory: alpha-amanitin
-
additional information
-
overview
-
additional information
-
overview
-
additional information
-
not inhibitory: alpha-amanitin
-
additional information
-
not inhibitory: 3-formalrifamycin SV:o-methyloxime; not inhibitory: 4-(dimethylamino)-4-deoxyrifamycin SV
-
additional information
-
Fip1, a component of yeast polyadenylation factor I, has an inhibitory effect on the enzyme activity because it competes with RNA for access to the C-RBS region
-
additional information
Fippbd peptide does not inhibit Pap1 activity even at concentrations in excess of 0.2 mM
-
additional information
-
Fippbd peptide does not inhibit Pap1 activity even at concentrations in excess of 0.2 mM
-
additional information
-
not inhibitory: alpha-amanitin
-
additional information
-
overview
-
additional information
-
cytoplasmic polyadenylation elements and PUF-binding elements are required for repression of GLD-2 mRNA
-
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0.0197
2-aminopurine riboside triphosphate
-
0.00039
oligo(A)12
-
incubation 30 min at 30 °C
-
0.0005 - 0.037
oligo(A)14
-
0.0263
oligo(A)17C
-
incubation at 30 °C for 15 min in the presence of MgATP2-
-
0.0468 - 0.0642
oligo(A)18
-
0.2
oligoadenylate
-
in presence of Mg2+, pH 9.0, 35°C
additional information
additional information
-
0.00092
(A)15
wild-type, pH 7.5, 37°C
0.00319
(A)15
mutant K560E, pH 7.5, 37°C
0.00534
(A)15
C-terminal deletion mutant, pH 7.5, 37°C
0.0468
(A)n
wild-type, pH 7.0, 30°C
0.106
(A)n
mutant N189A, pH 7.0, 30°C
0.195
(A)n
mutant K215A, pH 7.0, 30°C
0.367
(A)n
mutant N226A, pH 7.0, 30°C
0.711
(A)n
mutant Y224F, pH 7.0, 30°C
0.028
ATP
-
37°C, pH 8.0
0.03
ATP
-
polymerase IIa, 37°C
0.036
ATP
wild-type, pH 7.0, 30°C
0.0469
ATP
mutant K560E, pH 7.5, 37°C
0.05
ATP
-
p(A)3 primer, Mn2+-activated calf thymus enzyme
0.05
ATP
-
oligoadenylate (in presence of Mn2+)
0.05
ATP
-
polymerase IIb, 37°C
0.0636
ATP
wild-type, pH 7.5, 37°C
0.0643
ATP
C-terminal deletion mutant, pH 7.5, 37°C
0.08
ATP
mutant N189A, pH 7.0, 30°C
0.123
ATP
-
incubation at 30 °C for 15 min, using oligo(A)17C (a modification of the 3'-terminal residue from A to C)
0.13
ATP
-
incubation 30 min at 30 °C
0.143
ATP
-
major poly(A) polymerase, 37°C, pH 8.0
0.154
ATP
-
mutant D167N/N202A
0.229
ATP
-
wild-type, reactions are started with the addition of PAP and incubated at 37 °C for 15 minutes. Reactions are stopped by the addition of 8 microL of stop buffer (formamide with trace amount of bromophenol blue dye)
0.249
ATP
mutant N226A, pH 7.0, 30°C
0.4
ATP
-
major poly(A) polymerase, 37°C, pH 8.0
0.406
ATP
mutant K215A, pH 7.0, 30°C
0.627
ATP
-
mutant D167N/T317G
0.929
ATP
mutant Y224F, pH 7.0, 30°C
0.1036
CTP
-
-
0.104
CTP
wild-type, pH 7.0, 30°C
0.14
CTP
mutant N226A, pH 7.0, 30°C
0.148
CTP
mutant N189A, pH 7.0, 30°C
0.27
CTP
-
incubation 30 min at 30 °C
0.368
CTP
mutant K215A, pH 7.0, 30°C
4.7
CTP
mutant Y224F, pH 7.0, 30°C
0.055
GTP
mutant N226A, pH 7.0, 30°C
0.062
GTP
wild-type, pH 7.0, 30°C
0.0005
oligo(A)14
-
wild-type PAP, incubation at 30 °C
-
0.006
oligo(A)14
-
mutant Y224S
-
0.015
oligo(A)14
-
mutant Y224F
-
0.028
oligo(A)14
-
mutant N226A
-
0.037
oligo(A)14
-
mutant K215A
-
0.0468
oligo(A)18
-
incubation at 30 °C for 15 min in the presence of MgATP2-
-
0.0642
oligo(A)18
-
incubation at 30 °C for 15 min in the presence of MgCTP2-
-
0.01
oligo(A)n
-
Mn2+-activated enzyme, pH 8.3, 37°C
-
0.3
oligo(A)n
-
Mg2+-activated enzyme, pH 8.3, 37°C
-
0.0036
poly(A)n
-
Mn2+-activated enzyme, pH 8.3, 37°C
-
0.14 - 0.36
poly(A)n
-
Mg2+-activated enzyme, pH 8.3, 37°C
-
0.51
RNA (A)15
-
mutant A319R
-
0.74
RNA (A)15
-
mutant K232A
-
1.34
RNA (A)15
-
wild-type
-
1.43
RNA (A)15
-
mutant K228A
-
1.47
RNA (A)15
-
mutant V154A
-
1.88
RNA (A)15
-
mutant Q323A
-
2.63
RNA (A)15
-
mutant Y237A
-
2.8
RNA (A)15
-
mutant V206A
-
3.13
RNA (A)15
-
mutant T317G
-
5.31
RNA (A)15
-
mutant K158A
-
6.94
RNA (A)15
-
mutant N239A
-
7.32
RNA (A)15
-
mutant V156A
-
9.85
RNA (A)15
-
mutant V247A
-
10.21
RNA (A)15
-
mutant R199A
-
11.16
RNA (A)15
-
mutant V247R
-
11.44
RNA (A)15
-
mutant N202A
-
12.72
RNA (A)15
-
mutant G203H
-
13.15
RNA (A)15
-
mutant D167N
-
14.37
RNA (A)15
-
mutant F100D
-
16.41
RNA (A)15
-
mutant D167N/N202A
-
18.82
RNA (A)15
-
mutant D167N/T317G
-
22.84
RNA (A)15
-
mutant D167N/V247R
-
24.99
RNA (A)15
-
mutant F153A
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Coturnix sp.
-
-
-
additional information
additional information
-
dependence on divalent cation concentration
-
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malfunction
double isoform Gld2/Gld4 depletion results in a strong deficit in theta burst stimulation-long term potentiation and an enhancement of N-methyl-D-aspartate receptor-dependent long term depression. Gld4 depletion has negligible effects on hippocampal-dependent behaviors
malfunction
enzyme deficiency leads to reduced expression of haploid-specific mRNAs, spermiogenesis arrest and male infertility
malfunction
enzyme depletion not only reduces GLUT1 poly(A) tail length, but also GLUT1 protein. Enzyme depletion impairs glucose deprivation-induced GLUT1 up-regulation
malfunction
enzyme knock-out is lethal. Knock-down of enzyme induces apoptosis and restricts protein synthesis
malfunction
enzyme knockdown reduces mitophagosome formation
malfunction
enzyme knockout mice display reduced blood hemoglobin levels and activated primary B lymphocytes proliferate faster
malfunction
enzyme-deficient mice exhibit spermiogenesis arrest and male infertility. Enzyme loss has no impact either on the abundance of chromatoid body components such as PIWIL1, TDRD6, YBX2, and piRNAs, or on retrotransposon expression
malfunction
isoform Gld2 depletion from the mouse hippocampus results in a deficit in long term potentiation. Double isoform Gld2/Gld4 depletion results in a strong deficit in theta burst stimulation-long term potentiation and an enhancement of N-methyl-D-aspartate receptor-dependent long term depression. Gld2 depletion has negligible effects on hippocampal-dependent behaviors
malfunction
null mutations in isoform PAPS1 result in a male gametophytic defect
malfunction
reduced isoform PAPS1 activity leads to flowering-time defects
malfunction
reduced isoform PAPS4 activity leads to flowering-time defects
metabolism
-
nuclear enzyme isoforms regulate transcript abundance genome-wide. Isoform Star-PAP-specific polyadenylation site usage regulates the expression of the eukaryotic translation initiation factor EIF4A1, the tumor suppressor gene PTEN and the long non-coding RNANEAT1. Isoform Star-PAP-mediated alternative polyadenylation of PTEN is essential for DNA damage-induced increase of PTEN protein levels
metabolism
the enzyme is involved in non-templated 3'-adenylation of miRNAs
physiological function
depletion of isoform Gld2 promotes rather than inhibits p53 mRNA polyadenylation/translation, induces premature senescence and enhances the stability of cytoplasmic polyadenylation element binding protein CPEB mRNA. TheCPEB 3' untranslated region contains two miR-122 binding sites, which when deleted, elevate mRNA translation. miR-122 is present in primary fibroblasts and destabilizes by Gld2 depletion
physiological function
isoform GLD4 regulates p53 polyadenylation/translation in a cytoplasmic polyadenylation element binding protein CPEB dependent manner
physiological function
knockdown of GLD2 transcripts causes male sterility, as GLD2-deficient males do not produce mature sperm. Spermatogenesis up to and including meiosis appears normal in the absence of GLD2, but post-meiotic spermatid development rapidly becomes abnormal. Nuclear bundling and F-actin assembly are defective in GLD2 knockdown testes and nuclei fail to undergo chromatin reorganization in elongated spermatids. GLD2 also affects the incorporation of protamines and the stability of dynamin and transition protein transcripts
physiological function
removal of either isoform GLD-2 or RNA-binding protein RNP-8 results in shortened poly(A) tails and lowers abundance of four target-mRNAs, i.e. oma-2, egg-1, pup-2, andtra-2. GLD-2 depletion also lowers the abundance of most GLD-2/RNP-8 putative target-mRNAs when assayed on microarrays. The GLD-2/RNP-8 complex is a broad-spectrum regulator of the oogenesis program that acts within an RNA regulatory network to specify and produce fully functional oocytes
physiological function
silencing of a few endogenous heterochromatic genes depends on isoform Cid14. The majority of these are subtelomeric genes
physiological function
a strong loss-of-function mutation in PAPS1 causes a male gametophytic defect, whereas a weak allele leads to reduced leaf growth that results in part from a constitutive pathogen response. Polyadenylation of SMALL AUXIN UP RNA (SAUR) mRNAs depends specifically on PAPS1 function. The resulting reduction in SAUR activity in PAPS1 mutants contributes to their reduced leaf growth
physiological function
-
a terminal poly(A) tail is important for a subset of intron excision events that follow cleavage and polyadenylation. In these cases, splicing is promoted by the nuclear poly(A) binding protein, PABPN1, and poly(A) polymerase, PAP. Poly(A) polymerase is needed for efficient splicing. Inefficient polyadenylation is associated with impaired recruitment of splicing factors to affected introns, which are consequently degraded by the exosome
physiological function
inactivation of PAP-dependent hyperadenylation in cells leads to the upregulation of various ncRNAs, including snoRNA host genes, primary miRNA transcripts, and promoter upstream antisense RNAs. mRNAs with retained introns are susceptible to PABPN1 and PAPalpha/gamma-mediated decay. Transcripts are targeted for degradation due to inefficient export, a consequence of reduced intron number or incomplete splicing. A genetically-encoded poly(A) tail is sufficient to drive decay. Treatment with transcription inhibitors uncouples polyadenylation from decay, leading to runaway hyperadenylation of nuclear decay targets
physiological function
isoform PAPS1 plays a role in the connection between organ identity and growth patterns. Overgrowth of PAPS1 mutant petals is due to increased recruitment of founder cells into early organ primordia. The leaf phenotype of PAPS1 mutants is dominated by a constitutive immune response that leads to increased resistance to the biotrophic oomycete Hyaloperonospora arabidopsidis and reflects activation of the salicylic acid-independent signalling pathway downstream of ENHANCED DISEASE SUSCEPTIBILITY1(EDS1)/PHYTOALEXIN DEFICIENT4 (PAD4)
physiological function
mature tRNAs, which are normally not substrates for PAP I in wild-type cells, are rapidly polyadenylated as PAP I levels increase upon overexpression, leading to dramatic reductions in the fraction of aminoacylated tRNAs, cessation of protein synthesis and cell death. The toxicity associated with PAP I is exacerbated by the absence of either RNase T and/or RNase PH. Regulation of PAP I is critical not for preventing the decay of mRNAs, but rather for maintaining normal levels of functional tRNAs and protein synthesis
physiological function
nuclear RNA-dependent ATPase Mtr4 and either the nuclear non-canonical poly(A) polymerases, Trf4 or Trf5 assemble into a Trf4/5Air1/2/Mtr4 polyadenylation complex TRAMP. Disrupting the Mtr4/Trf interaction disrupts specific TRAMP and exosome functions, including small nucleolar RNA processing. A 20 amino acid peptide, residues 98-117 in the N-terminus of Trf5 is important for TRAMP complex formation
physiological function
plants lacking both isoforms PAPS2 and PAPS4 function are viable with wild-type leaf growth
physiological function
processing of the common precursor releases an incomplete tRNATyr lacking the 3'-adenosine which has to be added before addition of the CCA end and subsequent aminoacylation. Mitochondrial poly(A) polymerase mtPAP is responsible for this A addition. Complete repair can be reconstituted in vitro with three enzymes: mtPAP frequently adds more than one A to the 3'-end of the truncated tRNA, and either the mitochondrial deadenylase PDE12 or the endonuclease RNase Z trims the oligo(A) tail to a single A before CCA addition
physiological function
the trypanosome polyadenylation complex includes homologues to all four cleavage and polyadenylation specificity factor subunits, Fip1, CstF50/64, and Symplekin. Most of these factors are essential for growth and required for both in vivo polyadenylation and trans splicing
physiological function
autophagy receptor NDP52 and the enzyme form an autophagy receptor complex, which enhances autophagic elimination of damaged mitochondria
physiological function
ectopic enzyme expression inhibits proliferation as well as colony-forming ability of breast cancer cells. By regulating the expression of BCL2-interacting killer, the enzyme induces apoptosis of breast cancer cells through the mitochondrial pathway
physiological function
enzyme-mediated translational control of GLUT1 mRNA is dependent of an RNA binding protein, CPEB1, and its binding elements in the 3_UTR. Through regulating GLUT1 level, the enzyme affects glucose uptake into cells and lactate levels. The enzyme affects glucose-dependent cellular phenotypes such as migration and invasion in glioblastoma cells
physiological function
isoform Gld2 is essential for normal synaptic efficacy at least in the dentate gyrus of the hippocampus. Isoform Gld2 controls RNA processing, particularly exon skipping
physiological function
isoform Gld4 controls RNA processing, particularly exon skipping
physiological function
isoform PAPS promotes flowering in a partially redundant manner. The enzymes act antagonistically to isoform PAPS1, which delays the transition to flowering
physiological function
isoform PAPS1 interacts with the RNA-directed DNA-methylation pathway in sporophyte and pollen development. The enzyme is essential for pollen differentiation and function. Isoform PAPS1 and RDR6 function are required for transmitting-tract development
physiological function
isoform PAPS4 promotes flowering in a partially redundant manner. The enzyme acts antagonistically to isoform PAPS1, which delays the transition to flowering. Increased expression of isoform PAPS4 is sufficient to cause premature flowering
physiological function
the enzyme acts as an onco-suppressor with the specificity for B-lymphocyte lineage from which multiple myeloma originates. The enzyme controls survival and proliferation of multiple myeloma cells
physiological function
the enzyme is essential for spermatogenesis through its adenylation activitiy
physiological function
the enzyme is indispensable for the viability of human embryonic stem cells
physiological function
the enzyme is strongly induced during activation of primary splenocytes
physiological function
the enzyme regulates gene expression and probably plays a critical role during cell differentiation. Isoform FAM46C is a causal driver of multiple myeloma
physiological function
the enzyme regulates gene expression and probably plays a critical role during cell differentiation. The enzyme gene may be involved in the development of major malignancies including lung, colorectal, hepatocellular, head and neck, urothelial, endometrial and renal papillary carcinomas and melanoma
physiological function
the enzyme regulates spermiogenesis through a pathway distinct from that mediated by chromatoid body-associated factors
physiological function
-
silencing of a few endogenous heterochromatic genes depends on isoform Cid14. The majority of these are subtelomeric genes
-
physiological function
Trypanosoma brucei brucei 927 / 4 GUTat10.1 / TREU927
-
the trypanosome polyadenylation complex includes homologues to all four cleavage and polyadenylation specificity factor subunits, Fip1, CstF50/64, and Symplekin. Most of these factors are essential for growth and required for both in vivo polyadenylation and trans splicing
-
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120000 - 140000
-
Mg2+-activated enzyme, gel filtration
140000 - 160000
-
gel filtration
145000
-
polymerase IIa, gel filtration
145000 - 155000
-
gel filtration
150000
-
above, mouse L-cells, gel filtration
155000
-
polymerase IIb, gel filtration
180000
-
corresponds to the PAP protein encoded by gene CG15737, SDS-PAGE
185000
-
adenylyltransferase A, glycerol density gradient sedimentation
200000
-
small ubiquitin-like modifier-2/3-modified forms of PAP, SDS-PAGE
30000
-
4 * 30000, SDS-PAGE
35000
-
1 * 51000 + 1 * 35000, SDS-PAGE
43000
-
polymerase Ia and Ib, gel filtration
45000 - 60000
-
sedimentation analysis
51000
-
1 * 51000 + 1 * 35000, SDS-PAGE
65000
-
embryo, sedimentation analysis, gel filtration
65000 - 70000
-
gel filtration
76990
-
predicted from nucleotide sequence
82400
-
predicted from nucleotide sequence
82800
x * 83000, SDS-PAGE, x * 82800, deduced from gene sequence
83000
x * 83000, SDS-PAGE, x * 82800, deduced from gene sequence
86000
-
gel filtration, major poly(A) polymerase
94000
x * 94000, SDS-PAGE
95000
-
polymerase II, gel filtration
additional information
-
heterogenous, monomers to very large aggregates, all forms being active, gel filtration, recombinant protein
37000
-
gel filtration, minor poly(A) polymerase
37000
-
1 * 37000 + 1 * 57000, SDS-PAGE
48000
-
x * 48000, rat liver nucleoplasm, denaturing gel electrophoresis
48000
-
x * 48000, liver enzyme, SDS-PAGE
50000
-
1 * 50000, SDS-PAGE
50000
-
1 * 50000, nuclear Mn2+- and Mg2+-activated enzyme, SDS-PAGE
50000
-
x * 50000, heterogenous, monomers to very large aggregates, all forms being active, SDS-PAGE, gel filtration, recombinant protein
50000
-
x * 50000, Mg2+-activated, denaturing gel electrophoresis
50000
-
x * 50000, denaturing gel electrophoresis
50000 - 60000
-
gel filtration
50000 - 60000
-
enzymes NE PAP I and II, S100 PAP, sucrose density gradient sedimentation
54000
-
Gld-2
54000
-
x * 54000, SDS-PAGE
57000
-
glycerol density gradient centrifugation
57000
-
and 60000, 2 major forms of enzyme, gel filtration
57000
-
1 * 37000 + 1 * 57000, SDS-PAGE
58000
-
-
58000
-
nuclear Mg2+- and Mn2+-stimulated enzyme, glycerol density gradient sedimentation
58000
-
Mg2+-activated enzyme, sedimentation analysis
58000
-
adenylyltransferase B, glycerol density gradient sedimentation
60000
-
-
60000
-
Mn2+-activated enzyme, sedimentation analysis, gel filtration
60000
-
and 57000, 2 major forms of enzyme, gel filtration
60000
-
mitochondria, glycerol density gradient centrifugation
60000
-
1 * 85000 + 1 * 60000, SDS-PAGE
60000
-
x * 60000, hepatoma enzyme, SDS-PAGE
62000
-
-
62000
-
sucrose density gradient sedimentation, gel filtration
63000
-
Mn2+-activated, sedimentation analysis
63000
-
cytoplasmic Mn2+-dependent enzyme, glycerol density gradient sedimentation
63000
-
1 * 63000, SDS-PAGE
63000
-
x * 63000, SDS-PAGE
64000
-
1 * 64000, SDS-PAGE
64000
-
1 * 64000, SDS-PAGE
70000
-
gel filtration
70000
-
enzyme from infected cytoplasm, glycerol density gradient sedimentation
70000
-
x * 70000, SDS-PAGE
75000
-
1 * 75000, cytoplasmic, Mn2+-dependent enzyme, SDS-PAGE
75000
-
x * 75000, Mn2+-activated, denaturing gel electrophoresis
80000
-
sucrose density gradient sedimentation
80000
-
sucrose density gradient sedimentation
80000
-
x * 80000, SDS-PAGE
85000
-
1 * 85000 + 1 * 60000, SDS-PAGE
85000
-
x * 85000, SDS-PAGE, recombinant enzyme
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heterodimer
-
a distinct RNA-binding protein, GLD-3, binds to GLD-2 and stimulates its polyadenylation activity in vitro
heterotrimer
-
the large PAP subunit AMV038 functions alone to produce short poly(A) tails, the small PAP-subunit AMV060 exhibits 2'-O-methyltransferase activity
tetramer
-
4 * 30000, SDS-PAGE
?
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x * 70000, SDS-PAGE
?
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x * 85000, SDS-PAGE, recombinant enzyme
?
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x * 50000, heterogenous, monomers to very large aggregates, all forms being active, SDS-PAGE, gel filtration, recombinant protein
?
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x * 50000, denaturing gel electrophoresis
?
x * 83000, SDS-PAGE, x * 82800, deduced from gene sequence
?
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x * 50000, Mg2+-activated, denaturing gel electrophoresis
?
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x * 75000, Mn2+-activated, denaturing gel electrophoresis
?
x * about 60000, SDS-PAGE
?
x * about 60000, His-Sumo-tagged enzyme, SDS-PAGE
?
x * about 60000, His-Sumo-tagged enzyme, SDS-PAGE
?
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x * 60000, hepatoma enzyme, SDS-PAGE
?
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x * 48000, rat liver nucleoplasm, denaturing gel electrophoresis
?
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x * 48000, liver enzyme, SDS-PAGE
dimer
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1 * 85000 + 1 * 60000, SDS-PAGE
dimer
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1 * 51000 + 1 * 35000, SDS-PAGE
dimer
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1 * 37000 + 1 * 57000, SDS-PAGE
monomer
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1 * 62000, SDS-PAGE
monomer
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1 * 57000, SDS-PAGE
monomer
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1 * 60000, Mn2+-activated enzyme, denaturing gel electrophoresis
monomer
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1 * 50000, SDS-PAGE
monomer
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1 * 75000, cytoplasmic, Mn2+-dependent enzyme, SDS-PAGE
monomer
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1 * 50000, nuclear Mn2+- and Mg2+-activated enzyme, SDS-PAGE
monomer
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1 * 60000, SDS-PAGE
monomer
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1 * 64000, SDS-PAGE
monomer
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1 * 63000, SDS-PAGE
monomer
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1 * 64000, SDS-PAGE
additional information
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binding of enzyme to nuclear poly(A) binding protein results in 80-fold increase in apparent affinity for RNA, mechanism
additional information
dimerization is required for the catalytic activity of isoform PAPD1
additional information
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dimerization is required for the catalytic activity of isoform PAPD1
additional information
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enzyme interacts directly with cleavage factor I, implications for assembly of the processing complex and regulation of enzyme
additional information
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polynucleotide adenylyltransferase Trf5p is part of a complex similar to TRAMP complex and with overlapping functions
additional information
Pap1 N-terminus interacts with the first 300 amino acids of Pta1 and with Cft1, two subunits of the cleavage/polyadenylation factor, in which Pap1 resides, and with nucleic-acid binding proteins Nab6 and Sub1with known links to 30 end processing
additional information
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Pap1 N-terminus interacts with the first 300 amino acids of Pta1 and with Cft1, two subunits of the cleavage/polyadenylation factor, in which Pap1 resides, and with nucleic-acid binding proteins Nab6 and Sub1with known links to 30 end processing
additional information
isoform Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex. Helicase Mtr4, Cid14, and Air1 form a TRAMP-like complex. Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors.No physical link to chromatin has been identified
additional information
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isoform Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex. Helicase Mtr4, Cid14, and Air1 form a TRAMP-like complex. Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors.No physical link to chromatin has been identified
additional information
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isoform Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14-Air1 complex. Helicase Mtr4, Cid14, and Air1 form a TRAMP-like complex. Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors.No physical link to chromatin has been identified
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Crystals of PAP complexed to 3'-dATP and Mn2+ are grown from a solution made of 22% (w/v) polyethylene glycol 8000, 100 mM Mes (pH 6), 120 mM ammonium sulfate, 5 mM CaCl2, 2 mM MnCl2, and 2 mM beta-mercaptoethanol. Cocrystallization of PAP with 3'-dATP and MgCl2 is performed under conditions similar to those reported, with the exception that 5 mM MgCl2 is used instead of 2 mM MnCl2. Crystals are of the space group p212121, with one monomer per asymmetric unit and a solvent content of ~55%.
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in complex with an ATP analog
mutant C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V in complex with a chemically modified RNA, to 2.25 A resolution
core complex of isoform GLD-2 and RRM RNA binding domain protein RNP-8, to 2.5 A resolution. RNP-8 embraces the poly(A)-polymerase, docking onto several conserved hydrophobic hotspots present on the GLD-2 surface. RNP-8 stabilizes GLD-2 and indirectly stimulates polyadenylation. RNP-8 differs in amino-acid sequence and structure from GLD-2 binding partner GLD-3 but binds the same surfaces of GLD-2 by forming alternative interactions
germ-line development defective GLD-2GLD-3 complex up-regulates the expression of genes required for meiotic progression. The structure of a minimal polyadenylation complex that includes the conserved nucleotidyl-transferase core of GLD-2 and the N-terminal domain of GLD-3, to 2.3 A resolution, shows that the N-terminal domain of GLD-3 does not fold into the predicted multi-K homology domain but wraps around the catalytic domain of GLD-2. GLD-3 activates GLD-2 both indirectly by stabilizing the enzyme and directly by contributing positively charged residues near the RNA-binding cleft. Due to distinct structural features, GLD-2 displays unusual specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end
mature enzyme, to 1.82 A resolution. Enzyme crystallizes as a dimer and consists of a N-terminal domain (NTD: 52-194 aa) and of palm (195-341 aa) and fingers (342-527 aa). The palm domain harbors the catalytic triad, residue D237, located at the base of sheet beta6, D239 on strand beta6 and D319, which belongs to beta10. Structures of mtPAP in complex with cosubstrates UTP, CTP and GTP indicate that initial nucleotide selection occurs in the absence of a template
isoform PAPgamma bound to cordycepin triphosphate (3?dATP) and Ca2+, to 2.8 A resolution. One 3'-dATP and one Ca2+ are present in the active site of each PAP molecule. Strictly conserved catalytic residues Asp112 and Asp114 interact with Ca2+, which also ligates three non-bridging oxygens of the alpha, beta and gamma phosphates of 3'-dATP. PAPgamma closely resembles its PAPalpha ortholog
mutant D325A, to 3.1 A resolution. The overall structure of the palm and fingers domains is similar to that in the canonical poly(A) polymerases. The active site is located at the interface between the two domains, with a large pocket that can accommodate the substrates. The structure reveals a domain in the N-terminal region of PAPD1, with a backbone-fold that is similar to that of RNP-type RNA binding domains. This domain, together with a beta-arm insertion in the palm domain, contributes to dimerization of PAPD1. The crystal structure reveals a dimer, formed by the two molecules in the asymmetric unit
alone and in complex with 3-dATP
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hanging drop vapour diffusion method, using 20% (w/v) PEG 8000, 100 mM magnesium acetate, 100 mM imidazole (pH 6.2), 3% ethylene glycol
mutant D154A in complex with MgATP-RNA, hanging drop vapour diffusion method, in 0.1 M bis-Tris propane, pH 6.4, 0.2 M Li-acetate, and 16% PEG 3350
mutant D154A, trapped in complex with ATP and a five residue poly(A). Enzyme has undergone significant domain movement and shows a closed conformation with extensive interactions between substrates and all three polymerase domains
tethered to the 3'-end processing complex via Fip1 peptide, hanging drop vapour diffusion method, with 100 mM MES, pH 6.5, 8-10% PEG 20000
ATP-gamma-S bound and unbound structures. Subunit VP55 residues of the active site make specific interactions with ATP-gamma-S. Concave surface of subunit VP55 docks the globular subunit VP39. Model of RNA primer binding shows that subunit VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface
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hanging drop vapor diffusion method, using 2% (w/v) tacsimate pH 5.0, 0.15 M sodium citrate tribasic dehydrate pH 5.6 and 10% (w/v) PEG 3350 at 10°C
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C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V
introduction of a Cys residue in a mutant lacking all endogenous Cys residues. Mutant achieves maximum specific disulfide cross-linking efficiency. The resulting construct is active and, when mixed with a chemically modified RNA, yields crystals of an enzyme-RNA complex
C36S/C118V/C160S/C197S/C257S/C293S/C204V
mutation of all seven endogenous cysteine residues. Mutant is able to bind RNA at a level similar to that of wild-type, but no longer forms nonspecific disulfide cross-links with the modified RNA
D167N
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strong reduction of catalytic efficiency
D167N/N202A
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sharp decrease in catalytic efficiency
D167N/T317G
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sharp decrease in catalytic efficiency
D167N/V247R
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sharp decrease in catalytic efficiency
F100D
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strong reduction of catalytic efficiency
G203H
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strong reduction of catalytic efficiency
K228A
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increase in Km for ATP
K232A
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increase in Km for ATP
N202A
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high Km value for RNA, strong reduction of catalytic efficiency, incorporates etheno-ATP and N1-methyl-ATP better than wild-type, but incorporates N6-methyl-ATP poorly
N239A
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kcat for ATP is reduced fourfold
R199A
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reduces kcat for RNA about 30-fold
T317G
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increase in Km for ATP, tolerates etheno-ATP and GTP, rejects N6-methyl-ATP
V156A
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strong reduction of catalytic efficiency
V247R
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kcat for ATP is reduced 2000-fold, strong reduction of catalytic efficiency
Y237A
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increase in Km for ATP
D170A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D212A
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
D214A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D79A
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disparity between Diphosphate release and AMP incorporation
D88A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D90A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
E211A
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
G74A
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disparity between Diphosphate release and AMP incorporation
G74P
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disparity between Diphosphate release and AMP incorporation
R215A
the mutation leads to a dramatic loss in nucleotide specificity and the formation of poly(N) tails
D237N
loss of activity. A heterodimer in which one monomer is active and the other is not retains activity
K112E
disruption of a a continuous positively charged surface formed upon dimerization, decrease in activity
K76E/K80E/K81E
disruption of a a continuous positively charged surface formed upon dimerization, decrease in activity
R272E
complete loss of activity
D124A
the mutant shows strongly reduced activity compared to the wild type enzyme
D126A
the mutant shows strongly reduced activity compared to the wild type enzyme
D325A
mutation of one of the conserved Asp residues in the active site, complete loss of activity. The mutant protein gives better quality crystals than the wild-type enzyme
D90A/D92A
catalytically inactive
E200A
the mutant shows strongly reduced activity compared to the wild type enzyme
G107A
the mutant shows strongly reduced activity compared to the wild type enzyme
H259A/K260A/I261A
mutation in beta-arm, mutant remains dimeric
H259A/K260A/I261A/H294A/F295A/P297A
mutations simultaneously disrupt both areas of contact in the dimer interface, mutant is a stable monomer in solution, complete loss of activity
H294A/F295A/P297A
mutation in helix alphaE, mutant exists in a monomer-dimer equilibrium
K560E
mutation in the C-terminal basic motif. About 20% of wild-type activity
S108A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y221A/F222A
mutation in helix alphaB, mutant exists in a monomer-dimer equilibrium
D114A
polyadenylation-defective mutant
D90A/D92A
catalytically inactive
S537A
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the mutant catalytic domain is not phosphorylated by ERK
V498Y/C485R
the mutant is unable to bind Fip1 but retains full polymerase activity
Y224S
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12-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
D170P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D170P
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no detectable AMP incorporation
D214P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D214P
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no detectable AMP incorporation
D88P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D88P
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no detectable AMP incorporation
D90P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D90P
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no detectable AMP incorporation
D154A
crystallization data, closed conformation with extensive interactions between substrates and all three polymerase domains
D154A
the mutant has a nearly identical melting temperature as wild type PAP
K215A
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74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
K215A
2- to 4fold increase in Km values
K215A
the mutant has a nearly identical melting temperature as wild type PAP
N189A
residue bridges the N and middle domains in the closed state
N189A
the mutant has a nearly identical melting temperature as wild type PAP
N226A
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74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme
N226A
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
N226A
the mutant has a nearly identical melting temperature as wild type PAP
Y224F
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30-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
Y224F
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
Y224F
altered melting temperature (44°C) compared to the wild type enzyme
additional information
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chimeras of CCA-adding enzyme and PAP were constructed
additional information
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enzyme knockout mutant, the mRNA levels of bolA, which is induced in response to many forms of stress, are reduced 2.5fold in stationary phase. Absence of enzyme enhances the RssB-mediated deltaS proteolysis specifically in starved cells
additional information
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enzyme PAP I variant with C-terminal His-tag can be phosphorylated both in vivo and in vitro. In vivo phosphorylation impairs activity of the enzyme
additional information
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reengineering of enzyme in order to function as (UG) adding enzyme. Double- and triple-mutants in residues 211, 212, 215 add 570 G residues to oligoA15 substrate
additional information
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hmtPAP knockdown mutant cells show decreased steady state levels of mtDNA-encoded proteins as well as deficient mitochondrial activities such as oxygen consumption rate
additional information
deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
additional information
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deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
additional information
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GLD-2 disruption does not affect the poly(A) tail elongation in oocytes
additional information
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the un-17 mutant carries a temperature-sensitive mutation in the gene encoding PAP
additional information
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deletion of C-terminal 31 amino acids has no effect, deletion of C-terminal 67 amino acids affects RNA binding, deletion of N-terminal 18 amino acids eliminates specific activity
additional information
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mutation of bovine residue N202 (equivalent to yeast N189) to alanine has essentially no effect on the apparent Km for ATP, but has a pronounced effect on the apparent Vmax, suggesting that this residue is particularly important in the recognition of the adenine of ATP
additional information
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strain lacking the Rrp6p component of the nuclear exosome accumulate polyadenylated forms of different ribosomal RNA precursors. This polyadenylation is reduced in strains lacking polynucleotide adenylyltransferase Trf5p and enhanced in strains overexpressing Trf5p
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