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DNA + H2O
LexA-DNA complexes
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detected by electrophoretical mobility shift assays, LexA repressor is the key regulatory protein of the DNA repair system, the SOS response. LexA is directly involved in SOS induction of the Staphylococcus aureus pathogenicity islands, SaPIs. LexA represses SaPI operon I containing ORF5, ORF7, 8 and 9
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Repressor LexA + H2O
LexA cleavage products
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DNA + H2O
DNA-loop + ?
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DNA + H2O
DNA-loop + ?
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DNA + H2O
DNA-loop + ?
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DNA + H2O
DNA-loop + ?
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DNA + H2O
DNA-loop + ?
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Repressor LexA + H2O
LexA cleavage products
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Repressor LexA + H2O
LexA cleavage products
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Repressor LexA + H2O
LexA cleavage products
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intermolecular cleavage reaction in which the C-terminal fragment of LexA acts as an enzyme to cleave other molecules of LexA
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Repressor LexA + H2O
LexA cleavage products
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Ser-119 is a nucleophile and Lys-156 is an activator
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additional information
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repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88
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additional information
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repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88
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additional information
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repressor LexA exhibits a RecA-independent and alkaline pH-dependent autoproteolytic cleavage. The autoproteolytic cleavage occurs at pH 8.5 and above, is stimulated by the addition of Ca2+ and in the temperature range of 3057°C. The cleavage occurs at the peptide bond between Ala84 and Gly85, and optimal cleavage requires the presence of Ser118and Lys159. Cleavage of Anabaena LexA is affected upon deletion of three amino acids, G86L87I88
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additional information
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LexA binds to dinBox1 and to half-site dinBox1b in the SOS boxes in the lysogenic promoter P1 of phage GIL01. The dinBox1 is a 14-bp long sequence in the P1 promoter region that is similar to the consensus LexA binding site in Bacillus subtilis (CGAAC(n)4GTTCG). Transcription from promoter P1 is regulated by host LexA and phage-borne factors
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additional information
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LexA binds to dinBox1 and to half-site dinBox1b in the SOS boxes in the lysogenic promoter P1 of phage GIL01. The dinBox1 is a 14-bp long sequence in the P1 promoter region that is similar to the consensus LexA binding site in Bacillus subtilis (CGAAC(n)4GTTCG). Transcription from promoter P1 is regulated by host LexA and phage-borne factors
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additional information
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LexA paralogue can activate transcription
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C-terminal fragment of lambda repressor cleaves the LexA substrate about as efficiently as does the lexA enzyme
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inhibits gene activation by the AraC protein
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RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair
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additional information
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LexA repressor coordinately controls about 20 unlinked genes comprising the bacterial SOS response, an inducible DNA repair system, these genes are necessary for functions as diverse as mutagenesis, DNA repair, recombionation, cell division, and prophage induction, SOS response is activated upon autoproteolysis of LexA repressor into its two separate domains
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additional information
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LexA repressor coordinately controls about 20 unlinked genes comprising the bacterial SOS response, an inducible DNA repair system, these genes are necessary for functions as diverse as mutagenesis, DNA repair, recombionation, cell division, and prophage induction, SOS response is activated upon autoproteolysis of LexA repressor into its two separate domains
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additional information
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interaction of enzyme with DNA motifs recA and yebG. Dissociation rate is 0.045 per s for recA and 0.13 per s for yebG with short-ranged binding potentials showing a stiff hydrogen-bonding network between protein and DNA
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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intact LexA dimerises by the carboxyterminal domain, and binds to DNA sequences via a helix-turn-helix in its amino-terminal domain. Upon self-cleavage between residues Ala84 and Gly85, LexA dissociates from its DNA targets (SOS boxes), causing the induction of the SOS regulon. Two distinct conformations of the LexA cleavage site region
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additional information
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RecA stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA. Hence, the conformational flexibility of unbound LexA is the key element in establishing a co-ordinated SOS response. While LexA exhibits diverse dissociation rates from operators, it interacts extremely rapidly with DNA target sites. Modulation of LexA activity changes the occurrence of persister cells in bacterial populations
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genome-wide mapping of LexA1 binding sites using ChIP-qPCR, determination of genes directly associated with LexA1 binding sites, overview. the LexA1 binding site is a 16 nt palindrome whose consensus is roughly CTnnACnnnnGTnnAG, it is present in all sequences shown to bind to LexA1 in serovar Copenhageni. Almost every peak of LexA1 binding is located upstream of a gene, in potential regulatory regions. LexA1-bound genes show decreased or no differential expression after DNA damage
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additional information
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genome-wide mapping of LexA1 binding sites using ChIP-qPCR, determination of genes directly associated with LexA1 binding sites, overview. the LexA1 binding site is a 16 nt palindrome whose consensus is roughly CTnnACnnnnGTnnAG, it is present in all sequences shown to bind to LexA1 in serovar Copenhageni. Almost every peak of LexA1 binding is located upstream of a gene, in potential regulatory regions. LexA1-bound genes show decreased or no differential expression after DNA damage
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additional information
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presence of LexA-Myc is present in cell-free extract from Mycobacterium tuberculosis expressing pKS04 but not pKS04mut1 or pEJMyc. The translational start site for LexA is upstream of residue 1, it is translated from a start codon 57 bp further upstream at the transcriptional start site
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additional information
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qualitative analysis of DNA-binding activities of MtLexA and its mutants, MtLexA binds to dsDNA with the consensus sequence GAAC-N4-GTTT/C. Modeling of the MtLexA-DNA complex, overview. The length of the flanking sequences of bound DNA does not affect DNA binding by LexA. Analysis of autocatalytic cleavage of MtLexA and enzyme mutants
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additional information
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qualitative analysis of DNA-binding activities of MtLexA and its mutants, MtLexA binds to dsDNA with the consensus sequence GAAC-N4-GTTT/C. Modeling of the MtLexA-DNA complex, overview. The length of the flanking sequences of bound DNA does not affect DNA binding by LexA. Analysis of autocatalytic cleavage of MtLexA and enzyme mutants
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additional information
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presence of LexA-Myc is present in cell-free extract from Mycobacterium tuberculosis expressing pKS04 but not pKS04mut1 or pEJMyc. The translational start site for LexA is upstream of residue 1, it is translated from a start codon 57 bp further upstream at the transcriptional start site
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additional information
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qualitative analysis of DNA-binding activities of MtLexA and its mutants, MtLexA binds to dsDNA with the consensus sequence GAAC-N4-GTTT/C. Modeling of the MtLexA-DNA complex, overview. The length of the flanking sequences of bound DNA does not affect DNA binding by LexA. Analysis of autocatalytic cleavage of MtLexA and enzyme mutants
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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involved in SOS response to DNA damage through recA-lexA regulon
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involved in SOS response to DNA damage through recA-lexA regulon
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involved in SOS response to DNA damage through recA-lexA regulon
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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LexA is a DNA-binding protein
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LexA is a DNA-binding protein
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LexA is a DNA-binding protein
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LexA interacts with its own promoter. LexA-orthologue binds as a dimer to 12 bp direct repeats containing a CTA-N9-CTA sequence conserved in two target genes, lexA and crhR. Recombinant LexA does not bind the crhR transcript, it binds non-specifically to RNA and consequently does not appear to exert its effect on gene expression at the post-transcriptional level. Recombinant LexA binds the crhR gene as a dimer
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LexA paralogue can activate transcription
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upon binding to aryl hydrocarbon receptor ligands, XDVs (recombinant aryl hydrocarbon receptors) act as functional transcription factors, independent of aryl hydrocarbon receptor nuclear translocator, to induce the expression of a reporter gene (LacZ) driven by a synthetic LexA-responsive promoter in the yeast strain L40
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additional information
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LexA binds a 14 bp palindromic motif with consensus sequence TGTTC-N4-GAACA, computational analysis of the recognition motif, comparative genomics analysis. The Verrucomicrobia LexA protein targets tandem binding sites in LexA promoters
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additional information
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Vibrio cholerae LexA coordinates CTX prophage gene expression, overview. CTXPhi genes require for virion production initiate transcription from the strong PA promoter, which is dually repressed in lysogens by the phage-encoded repressor RstR and the host-encoded SOS repressor LexA. RstR both positively and negatively autoregulates its own expression from this promoter. LexA is absolutely required for RstR-mediated activation of PR transcription. Mechanisms, detailed overview
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additional information
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LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain
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additional information
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LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain
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additional information
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additional information
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LexA binds to dinBox1 and to half-site dinBox1b in the SOS boxes in the lysogenic promoter P1 of phage GIL01. The dinBox1 is a 14-bp long sequence in the P1 promoter region that is similar to the consensus LexA binding site in Bacillus subtilis (CGAAC(n)4GTTCG). Transcription from promoter P1 is regulated by host LexA and phage-borne factors
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additional information
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LexA binds to dinBox1 and to half-site dinBox1b in the SOS boxes in the lysogenic promoter P1 of phage GIL01. The dinBox1 is a 14-bp long sequence in the P1 promoter region that is similar to the consensus LexA binding site in Bacillus subtilis (CGAAC(n)4GTTCG). Transcription from promoter P1 is regulated by host LexA and phage-borne factors
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additional information
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RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair
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additional information
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LexA repressor coordinately controls about 20 unlinked genes comprising the bacterial SOS response, an inducible DNA repair system, these genes are necessary for functions as diverse as mutagenesis, DNA repair, recombionation, cell division, and prophage induction, SOS response is activated upon autoproteolysis of LexA repressor into its two separate domains
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additional information
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LexA repressor coordinately controls about 20 unlinked genes comprising the bacterial SOS response, an inducible DNA repair system, these genes are necessary for functions as diverse as mutagenesis, DNA repair, recombionation, cell division, and prophage induction, SOS response is activated upon autoproteolysis of LexA repressor into its two separate domains
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additional information
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interaction of enzyme with DNA motifs recA and yebG. Dissociation rate is 0.045 per s for recA and 0.13 per s for yebG with short-ranged binding potentials showing a stiff hydrogen-bonding network between protein and DNA
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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Rhodobacter capsulatus LexA binds to the predicted promoter regions of lexA, recA, and cckA and represses cckA and recA transcription. Putative LexA binding sites are present 5' of SOS response gene homologues and the RcGTA regulatory gene cckA
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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involved in SOS response to DNA damage through recA-lexA regulon
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additional information
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Vibrio cholerae LexA coordinates CTX prophage gene expression, overview. CTXPhi genes require for virion production initiate transcription from the strong PA promoter, which is dually repressed in lysogens by the phage-encoded repressor RstR and the host-encoded SOS repressor LexA. RstR both positively and negatively autoregulates its own expression from this promoter. LexA is absolutely required for RstR-mediated activation of PR transcription. Mechanisms, detailed overview
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additional information
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LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain
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additional information
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LexA-gp7 interaction forms a heterohexamer with 2:4 stoichiometry. Gp7 interacts with Bacillus thuringiensis LexA C-terminal domain
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evolution
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evolutionary dynamics of the SOS response involving the LexA enzyme, overview. The composition of the SOS genetic network and the binding motif of its transcriptional repressor, LexA, vary greatly across bacterial clades. Multiple sequence alignment of available LexA protein sequences for the phylum Verrucomicrobia, using the information in Escherichia coli LexA cyrstal structure (UniProt ID P0A7C2). The core Verrucomicrobia LexA regulon comprises three operons involved in DNA repair and mutagenesis, i.e. lexA, splB, and imuA-imuB-dnaE2. The Verrucomicrobia LexA regulon is highly variable and incorporates novel functions, overview
malfunction
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Bacillus thuringenis LexA binds to dinBox sequences in the temperate phage GIL01, repressing phage gene expression during lysogeny and providing the switch necessary to enter lytic development
malfunction
a lexA deletion strain WP3DELTAlexA shows no growth defects at 4-20°C
malfunction
deletion of the lexA gene results in the abolition of detectable RcGTA production and an about 10fold reduction in recipient capability. Expression of gene cckA, encoding the sensor kinase CckA, is increased over 5fold in the lexA mutant, and a lexA/cckA double mutant is found to have the same phenotype as a DELTAcckA single mutant in terms of RcGTA production. The RcGTA-deficient phenotype of the lexA mutant is largely due to the overexpression of cckA. RcGTA transposon Tn5 mutagenesis, overview
malfunction
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a lexA deletion strain WP3DELTAlexA shows no growth defects at 4-20°C
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malfunction
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deletion of the lexA gene results in the abolition of detectable RcGTA production and an about 10fold reduction in recipient capability. Expression of gene cckA, encoding the sensor kinase CckA, is increased over 5fold in the lexA mutant, and a lexA/cckA double mutant is found to have the same phenotype as a DELTAcckA single mutant in terms of RcGTA production. The RcGTA-deficient phenotype of the lexA mutant is largely due to the overexpression of cckA. RcGTA transposon Tn5 mutagenesis, overview
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malfunction
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deletion of the lexA gene results in the abolition of detectable RcGTA production and an about 10fold reduction in recipient capability. Expression of gene cckA, encoding the sensor kinase CckA, is increased over 5fold in the lexA mutant, and a lexA/cckA double mutant is found to have the same phenotype as a DELTAcckA single mutant in terms of RcGTA production. The RcGTA-deficient phenotype of the lexA mutant is largely due to the overexpression of cckA. RcGTA transposon Tn5 mutagenesis, overview
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malfunction
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deletion of the lexA gene results in the abolition of detectable RcGTA production and an about 10fold reduction in recipient capability. Expression of gene cckA, encoding the sensor kinase CckA, is increased over 5fold in the lexA mutant, and a lexA/cckA double mutant is found to have the same phenotype as a DELTAcckA single mutant in terms of RcGTA production. The RcGTA-deficient phenotype of the lexA mutant is largely due to the overexpression of cckA. RcGTA transposon Tn5 mutagenesis, overview
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malfunction
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a lexA deletion strain WP3DELTAlexA shows no growth defects at 4-20°C
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metabolism
LexA-mediated repression of recA expression is a hallmark of the prototypical SOS response
metabolism
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LexA-mediated repression of recA expression is a hallmark of the prototypical SOS response
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metabolism
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LexA-mediated repression of recA expression is a hallmark of the prototypical SOS response
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metabolism
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LexA-mediated repression of recA expression is a hallmark of the prototypical SOS response
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physiological function
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LexA transcriptionally represses recA, LexA also functions as an auto-repressor. It is involved in the repair mechanism called the SOS response as a gene regulator, expression dynamics of various genes in the SOS system, overview
physiological function
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Vibrio cholerae LexA coordinates CTX prophage gene expression, overview. CTXPhi genes require for virion production initiate transcription from the strong PA promoter, which is dually repressed in lysogens by the phage-encoded repressor RstR and the host-encoded SOS repressor LexA. RstR both positively and negatively autoregulates its own expression from this promoter. LexA is absolutely required for RstR-mediated activation of PR transcription. Mechanisms, detailed overview
physiological function
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LexA regulated genes exhibit phenotypic heterogeneity as high level expression is observed in only a small subpopulation of cells. Heterogenous expression is established primarily by stochastic factors and the binding affinity of LexA to SOS boxes. In a lexA defective strain, high level expression of the regulated genes is observed in the large majority of the cells. The simultaneous expression of cka, encoding the pore forming colicin K, and lexA, investigated at the single cell level reveals high level expression of only cka in rare individual cells
physiological function
isozyme LexA1 is probably the main regulator of the SOS response in Leptospira interrogans. In addition to both lexA genes and their operons, recA, recN and dinP are LexA1-bound and induced by DNA damage. LexA1 binds to the upstream sequence of both lexA1 and lexA2. Global transcriptional profiling during UV-C DNA damage response, overview. Two prophages heavily induce 12 h after UV-C irradiation involving LexA1 binding. Determination of LexA1 SOS box and DNA damage-inducible LexA1-bound genes
physiological function
LexA is a central repressor in the SOS response. During infection of Bacillus thuringiensis with GIL01 bacteriophage, bacterial LexA represses the SOS response and the phage lytic cycle by binding DNA, the interaction is further stabilized upon binding of a viral protein, phage-borne gp7. Analysis of binding stoichiometry and potential interaction with LexA using surface plasmon resonance, static light scattering, and small-angle X-ray scattering, overview. LexA binds and represses expression through binding of dinBox1/1b, with LexA affinity for this region increased through interaction with a viral accessory protein gp7. Removal of the last six C-terminal residues of gp7 does not prevent its interaction with LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry. Under regular growth conditions, LexA binds SOS-box sequences upstream of DNA repair genes to suppress the expression of these genes
physiological function
LexA is a critical protein involved in the bacterial SOS response, which consists of the coordinated activation of a network of genes required for DNA repair and mutagenesis in response to DNA damage. The clinical relevance of the SOS response in bacteria can be attributed not only to its involvement in virulence and mutagenesis, but also in the spread of antibiotic resistance
physiological function
LexA is a DNA-binding protein and a SOS regulator. SOS is a formidable strategy used by bacteria against various environmental stresses. The LexA protein is a transcriptional regulator situated in the central position of the SOS pathway
physiological function
the LexA repressor, the master regulator of the SOS response in many bacteria, as a regulator of RcGTA activity. Gene transfer agent of Rhodobacter capsulatus (RcGTA) is a genetic exchange element that combines central aspects of bacteriophage-mediated transduction and natural transformation. RcGTA particles resemble a small double-stranded DNA bacteriophage, package random about 4-kb fragments of the producing cell genome, and are released from a subpopulation (below 1%) of cells in a stationary-phase culture. RcGTA particles deliver this DNA to surrounding Rhodobacter capsulatus cells, and the DNA is integrated into the recipient genome though a process that requires homologs of natural transformation genes and RecA-mediated homologous recombination. LexA is required for RcGTA production and maximal recipient capability, the regulation of RcGTA production is complex and involves several bacterial regulatory factors
physiological function
the SOS response in Eubacteria is a global response to DNA damage and its activation is increasingly associated with the movement of mobile genetic elements. The temperate phage GIL01, a parasite of the bacterium, is induced into lytic growth using the host's SOS response to genomic stress. LexA, the SOS transcription factor, represses bacteriophage transcription by binding to a set of SOS boxes in the lysogenic promoter P1. LexA is unable to efficiently repress GIL01 transcription unless the small phage-encoded protein gp7 is also present. Phage protein gp7 forms a stable complex with LexA that enhances LexA binding to phage and cellular SOS sites and interferes with RecA-mediated auto-cleavage of LexA, the key step in the initiation of the SOS response. Gp7 does not bind DNA, alone or when complexed with LexA. Gp7 interacts with LexA at dinBox1 and dinBox1b and Gp7 induces a LexA conformation that favors DNA binding but disfavors LexA auto-cleavage, thereby altering the dynamics of the cellular SOS response. Gp7 increases the apparent binding capacity of LexA for din-Box1 and dinBox1b
physiological function
-
the SOS response is the primary bacterial mechanism to address DNA damage, coordinating multiple cellular processes that include DNA repair, cell division, and translesion synthesis. In contrast to other regulatory systems, the composition of the SOS genetic network and the binding motif of its transcriptional repressor, LexA, vary greatly across bacterial clades
physiological function
-
LexA is a DNA-binding protein and a SOS regulator. SOS is a formidable strategy used by bacteria against various environmental stresses. The LexA protein is a transcriptional regulator situated in the central position of the SOS pathway
-
physiological function
-
the LexA repressor, the master regulator of the SOS response in many bacteria, as a regulator of RcGTA activity. Gene transfer agent of Rhodobacter capsulatus (RcGTA) is a genetic exchange element that combines central aspects of bacteriophage-mediated transduction and natural transformation. RcGTA particles resemble a small double-stranded DNA bacteriophage, package random about 4-kb fragments of the producing cell genome, and are released from a subpopulation (below 1%) of cells in a stationary-phase culture. RcGTA particles deliver this DNA to surrounding Rhodobacter capsulatus cells, and the DNA is integrated into the recipient genome though a process that requires homologs of natural transformation genes and RecA-mediated homologous recombination. LexA is required for RcGTA production and maximal recipient capability, the regulation of RcGTA production is complex and involves several bacterial regulatory factors
-
physiological function
-
isozyme LexA1 is probably the main regulator of the SOS response in Leptospira interrogans. In addition to both lexA genes and their operons, recA, recN and dinP are LexA1-bound and induced by DNA damage. LexA1 binds to the upstream sequence of both lexA1 and lexA2. Global transcriptional profiling during UV-C DNA damage response, overview. Two prophages heavily induce 12 h after UV-C irradiation involving LexA1 binding. Determination of LexA1 SOS box and DNA damage-inducible LexA1-bound genes
-
physiological function
-
the LexA repressor, the master regulator of the SOS response in many bacteria, as a regulator of RcGTA activity. Gene transfer agent of Rhodobacter capsulatus (RcGTA) is a genetic exchange element that combines central aspects of bacteriophage-mediated transduction and natural transformation. RcGTA particles resemble a small double-stranded DNA bacteriophage, package random about 4-kb fragments of the producing cell genome, and are released from a subpopulation (below 1%) of cells in a stationary-phase culture. RcGTA particles deliver this DNA to surrounding Rhodobacter capsulatus cells, and the DNA is integrated into the recipient genome though a process that requires homologs of natural transformation genes and RecA-mediated homologous recombination. LexA is required for RcGTA production and maximal recipient capability, the regulation of RcGTA production is complex and involves several bacterial regulatory factors
-
physiological function
-
LexA is a critical protein involved in the bacterial SOS response, which consists of the coordinated activation of a network of genes required for DNA repair and mutagenesis in response to DNA damage. The clinical relevance of the SOS response in bacteria can be attributed not only to its involvement in virulence and mutagenesis, but also in the spread of antibiotic resistance
-
physiological function
-
LexA is a critical protein involved in the bacterial SOS response, which consists of the coordinated activation of a network of genes required for DNA repair and mutagenesis in response to DNA damage. The clinical relevance of the SOS response in bacteria can be attributed not only to its involvement in virulence and mutagenesis, but also in the spread of antibiotic resistance
-
physiological function
-
LexA is a central repressor in the SOS response. During infection of Bacillus thuringiensis with GIL01 bacteriophage, bacterial LexA represses the SOS response and the phage lytic cycle by binding DNA, the interaction is further stabilized upon binding of a viral protein, phage-borne gp7. Analysis of binding stoichiometry and potential interaction with LexA using surface plasmon resonance, static light scattering, and small-angle X-ray scattering, overview. LexA binds and represses expression through binding of dinBox1/1b, with LexA affinity for this region increased through interaction with a viral accessory protein gp7. Removal of the last six C-terminal residues of gp7 does not prevent its interaction with LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry. Under regular growth conditions, LexA binds SOS-box sequences upstream of DNA repair genes to suppress the expression of these genes
-
physiological function
-
the LexA repressor, the master regulator of the SOS response in many bacteria, as a regulator of RcGTA activity. Gene transfer agent of Rhodobacter capsulatus (RcGTA) is a genetic exchange element that combines central aspects of bacteriophage-mediated transduction and natural transformation. RcGTA particles resemble a small double-stranded DNA bacteriophage, package random about 4-kb fragments of the producing cell genome, and are released from a subpopulation (below 1%) of cells in a stationary-phase culture. RcGTA particles deliver this DNA to surrounding Rhodobacter capsulatus cells, and the DNA is integrated into the recipient genome though a process that requires homologs of natural transformation genes and RecA-mediated homologous recombination. LexA is required for RcGTA production and maximal recipient capability, the regulation of RcGTA production is complex and involves several bacterial regulatory factors
-
physiological function
-
the SOS response in Eubacteria is a global response to DNA damage and its activation is increasingly associated with the movement of mobile genetic elements. The temperate phage GIL01, a parasite of the bacterium, is induced into lytic growth using the host's SOS response to genomic stress. LexA, the SOS transcription factor, represses bacteriophage transcription by binding to a set of SOS boxes in the lysogenic promoter P1. LexA is unable to efficiently repress GIL01 transcription unless the small phage-encoded protein gp7 is also present. Phage protein gp7 forms a stable complex with LexA that enhances LexA binding to phage and cellular SOS sites and interferes with RecA-mediated auto-cleavage of LexA, the key step in the initiation of the SOS response. Gp7 does not bind DNA, alone or when complexed with LexA. Gp7 interacts with LexA at dinBox1 and dinBox1b and Gp7 induces a LexA conformation that favors DNA binding but disfavors LexA auto-cleavage, thereby altering the dynamics of the cellular SOS response. Gp7 increases the apparent binding capacity of LexA for din-Box1 and dinBox1b
-
physiological function
-
LexA is a DNA-binding protein and a SOS regulator. SOS is a formidable strategy used by bacteria against various environmental stresses. The LexA protein is a transcriptional regulator situated in the central position of the SOS pathway
-
additional information
a complex of Mycobacterium tuberculosis LexA and the cognate SOS box is modeled in which the mutual orientation of the two N-terminal domains differs from that in the Escherichia coli LexA-DNA complex, complex structure analysis, overview
additional information
a monodisperse mixture of gp7 and LexA appears as a 72-kDa heterohexameric complex composed of a tetrameric gp7 and dimeric LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry
additional information
identification of putative Lex binding sites located 5' of typical SOS response coding sequences and also 5' of the RcGTA regulatory gene cckA, which encodes a hybrid histidine kinase homologue
additional information
-
identification of putative Lex binding sites located 5' of typical SOS response coding sequences and also 5' of the RcGTA regulatory gene cckA, which encodes a hybrid histidine kinase homologue
additional information
-
identification of putative Lex binding sites located 5' of typical SOS response coding sequences and also 5' of the RcGTA regulatory gene cckA, which encodes a hybrid histidine kinase homologue
-
additional information
-
identification of putative Lex binding sites located 5' of typical SOS response coding sequences and also 5' of the RcGTA regulatory gene cckA, which encodes a hybrid histidine kinase homologue
-
additional information
-
a complex of Mycobacterium tuberculosis LexA and the cognate SOS box is modeled in which the mutual orientation of the two N-terminal domains differs from that in the Escherichia coli LexA-DNA complex, complex structure analysis, overview
-
additional information
-
a complex of Mycobacterium tuberculosis LexA and the cognate SOS box is modeled in which the mutual orientation of the two N-terminal domains differs from that in the Escherichia coli LexA-DNA complex, complex structure analysis, overview
-
additional information
-
a monodisperse mixture of gp7 and LexA appears as a 72-kDa heterohexameric complex composed of a tetrameric gp7 and dimeric LexA. Modeling of LexA-gp7 interaction in which gp7 acts as a small scaffold to orient the N-terminal and C-terminal domains of LexA such that the binding affinity to DNA is increased. LexA-gp7 Interaction forms a heterohexamer with 2:4 stoichiometry
-
additional information
-
identification of putative Lex binding sites located 5' of typical SOS response coding sequences and also 5' of the RcGTA regulatory gene cckA, which encodes a hybrid histidine kinase homologue
-
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K156A
-
site directed mutagenesis
L89P/Q92W/E152A/K156A
-
designed to trap protein in conformation required for cleavage. Crystallization data of tryptic fragment containing amino acids 68202
G126D
site-directed mutagenesis, cleavage site mutant
K197A
site-directed mutagenesis, active site mutant
S160A
site-directed mutagenesis, active site mutant
G126D
-
site-directed mutagenesis, cleavage site mutant
-
K197A
-
site-directed mutagenesis, active site mutant
-
S160A
-
site-directed mutagenesis, active site mutant
-
G126D
-
site-directed mutagenesis, cleavage site mutant
-
K197A
-
site-directed mutagenesis, active site mutant
-
S160A
-
site-directed mutagenesis, active site mutant
-
G94E
-
prevents cleavage of the LexA
G85D
-
LexA mutant
G85D
-
change in cleavage site, that blocks autocleavage but has normal active site, crystallization data
S119A
-
LexA mutant
S119A
-
change in the active site, but normal cleavage site. Crystallization data of full length protein and of tryptic fragment containing amino acids 68202
S119A
-
site directed mutagenesis
S119A
-
one subunit is well-ordered throughout and in the non-cleavable state, whereas the second subunit, whilst disordered in the amino-terminal domain, adopts the cleavable state in the carboxy-terminal domain
additional information
-
deletion of lexA gene of strain ATCC 13032 to create the mutant strain NJ2114, which has an elongated cell morphology and an increased doubling time. Comparison of SOS regulon, the transcriptomes of NJ2114, and a DNA-damage-induced wild-type strain with the wild-type control using DNA microarray hybridization, overview
additional information
-
K156A, L89P, Q92W, E152A quadruple mutant, K156A, Q92W, E152A mutant variant -89, K156A, L89P, E152A mutant variant -92, K156A, L89P, Q92W mutant variant -152, K156A, Q92W mutant variant, Q92W S119A mutant variant, expression of truncated variants
additional information
construction of knockout mutant DELTAlexA mutant, the decrease in gene transfer frequency from the DELTAlexA mutant is associated with a decrease in transcription of the RcGTA structural gene cluster, the -galactosidase activities of WTand DELTAlexA mutant cells containing a plasmid with the RcGTA promoter fused to lacZ are compared. RcGTA recipient capability is decreased in the DELTAlexA mutant, phenotype, and morphology of DELTAlexA mutant cells, overview
additional information
-
construction of knockout mutant DELTAlexA mutant, the decrease in gene transfer frequency from the DELTAlexA mutant is associated with a decrease in transcription of the RcGTA structural gene cluster, the -galactosidase activities of WTand DELTAlexA mutant cells containing a plasmid with the RcGTA promoter fused to lacZ are compared. RcGTA recipient capability is decreased in the DELTAlexA mutant, phenotype, and morphology of DELTAlexA mutant cells, overview
additional information
-
construction of knockout mutant DELTAlexA mutant, the decrease in gene transfer frequency from the DELTAlexA mutant is associated with a decrease in transcription of the RcGTA structural gene cluster, the -galactosidase activities of WTand DELTAlexA mutant cells containing a plasmid with the RcGTA promoter fused to lacZ are compared. RcGTA recipient capability is decreased in the DELTAlexA mutant, phenotype, and morphology of DELTAlexA mutant cells, overview
-
additional information
-
construction of knockout mutant DELTAlexA mutant, the decrease in gene transfer frequency from the DELTAlexA mutant is associated with a decrease in transcription of the RcGTA structural gene cluster, the -galactosidase activities of WTand DELTAlexA mutant cells containing a plasmid with the RcGTA promoter fused to lacZ are compared. RcGTA recipient capability is decreased in the DELTAlexA mutant, phenotype, and morphology of DELTAlexA mutant cells, overview
-
additional information
-
construction of knockout mutant DELTAlexA mutant, the decrease in gene transfer frequency from the DELTAlexA mutant is associated with a decrease in transcription of the RcGTA structural gene cluster, the -galactosidase activities of WTand DELTAlexA mutant cells containing a plasmid with the RcGTA promoter fused to lacZ are compared. RcGTA recipient capability is decreased in the DELTAlexA mutant, phenotype, and morphology of DELTAlexA mutant cells, overview
-
additional information
-
introduction of a mutation recAo6869 in the LexA binding site, in the promoter region of the recA gene, leads to dramatically decreased fitness of orally but not intraperitoneally inoculated recAo6869 cells. However, the SOS response of this mutant is induced normally, and there is no increase in the sensitivity of the strain toward DNA-damaging agents, bile salts, or alterations in pH. Nevertheless, recAo6869 cells are unable to swarm and their capacity to cross the intestinal epithelium is significantly reduced, phenotype, detailed overview. The rate of RecA protein accumulation increases about 5fold in mitomycin C-treated wild-type cells, whereas no induction is observed in the lexA3(Ind) strain
additional information
-
introduction of a mutation recAo6869 in the LexA binding site, in the promoter region of the recA gene, leads to dramatically decreased fitness of orally but not intraperitoneally inoculated recAo6869 cells. However, the SOS response of this mutant is induced normally, and there is no increase in the sensitivity of the strain toward DNA-damaging agents, bile salts, or alterations in pH. Nevertheless, recAo6869 cells are unable to swarm and their capacity to cross the intestinal epithelium is significantly reduced, phenotype, detailed overview. The rate of RecA protein accumulation increases about 5fold in mitomycin C-treated wild-type cells, whereas no induction is observed in the lexA3(Ind) strain
-
additional information
construction of a lexA deletion strain WP3DELTAlexA, no growth defect is observed. 481 and 108 genes are differentially expressed at 20°C and 4°C, respectively, as demonstrated by comparative whole genome microarray analysis
additional information
-
construction of a lexA deletion strain WP3DELTAlexA, no growth defect is observed. 481 and 108 genes are differentially expressed at 20°C and 4°C, respectively, as demonstrated by comparative whole genome microarray analysis
-
additional information
-
construction of a lexA deletion strain WP3DELTAlexA, no growth defect is observed. 481 and 108 genes are differentially expressed at 20°C and 4°C, respectively, as demonstrated by comparative whole genome microarray analysis
-
additional information
-
site-directed mutagenesis of the Verrucomicrobium spinosum recA promoter confirms that LexA binds a 14 bp palindromic motif with consensus sequence TGTTC-N4-GAACA
additional information
-
construction of strain BW27784 sulA6209 lexA71, that lacks LexA activity
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Little, J.W.; Kim, B.; Roland, K.L.; Smith, M.H.; Lin, L.L.; Slilaty, S.N.
Cleavage of LexA repressor
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Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism
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Nucleotide sequence of the lexA gene of E. coli
Cell
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LexA and lambda Cl repressors as enzymes: specific cleavage in an intermolecular reaction
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Escherichia coli
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Improved Model of a LexA Repressor Dimer Bound to recA Operator
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Crystal structure of LexA: A conformational switch for regulation of self-cleavage
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2001
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Garriga, X.; Calero, S.; Barbe, J.
Nucleotide sequence analysis and comparison of the lexA genes from Salmonella typhimurium, Erwinia carotovora, Pseudomonas aeruginosa and Pseudomonas putida
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Escherichia coli, Pectobacterium carotovorum (Q04596), Pectobacterium carotovorum, Pseudomonas aeruginosa (P37452), Pseudomonas aeruginosa, Pseudomonas putida (P0A154), Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium (P0A273), Salmonella enterica subsp. enterica serovar Typhimurium
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2008
Escherichia coli, no activity in Streptococcus thermophilus
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SaPI operon I is required for SaPI packaging and is controlled by LexA
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2007
Staphylococcus aureus
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Lee, T.; James, M.N.
1.2.ANG.-resolution crystal structures reveal the second tetrahedral intermediates of streptogrisin B (SGPB)
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2008
Bacillus subtilis, Cereibacter sphaeroides, Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Synechocystis sp., Xanthomonas sp.
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Experimental determination of translational start sites resolves uncertainties in genomic open reading frame predictions - application to Mycobacterium tuberculosis
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2009
Mycobacterium tuberculosis (P9WHR7), Mycobacterium tuberculosis H37Rv (P9WHR7)
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Overexpression of the LexA-regulated tisAB RNA in E. coli inhibits SOS functions; implications for regulation of the SOS response
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2008
Escherichia coli
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2009
synthetic construct
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2010
Salmonella enterica, Salmonella enterica UA1876
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Vibrio cholerae LexA coordinates CTX prophage gene expression
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2009
Vibrio cholerae serotype O1
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Genetic makeup of the Corynebacterium glutamicum LexA regulon deduced from comparative transcriptomics and in vitro DNA band shift assays
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Corynebacterium glutamicum
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Stochastic analysis of the SOS response in Escherichia coli
PLoS ONE
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2009
Escherichia coli
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Chandran, A.; Prabu, J.; Manjunath, G.; Patil, K.; Muniyappa, K.; Vijayan, M.
Crystallization and preliminary X-ray studies of the C-terminal domain of Mycobacterium tuberculosis LexA
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66
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2010
Mycobacterium tuberculosis (P9WHR7), Mycobacterium tuberculosis H37Rv (P9WHR7)
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Novel insights into the regulation of LexA in the cyanobacterium Synechocystis sp. strain PCC 6803
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Bacillus thuringiensis
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Fornelos, N.; Butala, M.; Hodnik, V.; Anderluh, G.; Bamford, J.K.; Salas, M.
Bacteriophage GIL01 gp7 interacts with host LexA repressor to enhance DNA binding and inhibit RecA-mediated auto-cleavage
Nucleic Acids Res.
43
7315-7329
2015
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Schons-Fonseca, L.; Da Silva, J.; Milanez, J.; Domingos, R.; Smith, J.; Nakaya, H.; Grossman, A.; Ho, P.; Da Costa, R.
Analysis of LexA binding sites and transcriptomics in response to genotoxic stress in Leptospira interrogans
Nucleic Acids Res.
44
1179-1191
2016
Leptospira interrogans serovar Copenhageni (M3G1T5), Leptospira interrogans serovar Copenhageni LT2050 (M3G1T5)
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Caveney, N.A.; Pavlin, A.; Caballero, G.; Bahun, M.; Hodnik, V.; de Castro, L.; Fornelos, N.; Butala, M.; Strynadka, N.C.J.
Structural insights into bacteriophage GIL01 gp7 inhibition of host LexA repressor
Structure
27
1094-1102
2019
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