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Literature summary for 2.1.1.368 extracted from
- EHMT2 and SETDB1 protect the maternal pronucleus from 5mC oxidation (2019), Proc. Natl. Acad. Sci. USA, 166, 10834-10841 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | Q9Z148 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| oocyte | - |
Mus musculus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| EHMT2 | - |
Mus musculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | deletion of the catalytic domain of either histone methyltransferases EHMT2 or SETDB1 in growing oocytes leads to significant reduction of global H3K9me2 or H3K9me3 levels, respectively, in the maternal pronucleus. The asymmetry of global 5?methylcytosine (5mC) oxidation is significantly reduced in the zygotes that carry maternal mutation of either the Ehmt2 or Setdb1 genes. The levels of 5-hydroxymethylcytosine, 5-formylcytosine, and 5-carboxylcytosine increase, and 5mC levels decrease in the mutant maternal pronuclei. H3K9me3-rich rings around the nucleolar-like bodies retain 5mC in the maternal mutant zygotes. The maternal pronuclei expand in size in the mutant zygotes and contain a significantly increased number of nucleolar-like bodies compared with normal zygotes | Mus musculus |
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