rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
18
|
pubmed:dateCreated |
2004-9-21
|
pubmed:abstractText |
The C. elegans proteins MES-2 and MES-6, orthologs of the Polycomb group (PcG) chromatin repressors E(Z) and ESC, exist in a complex with their novel partner MES-3. The MES system participates in silencing the X chromosomes in the hermaphrodite germline. Loss of maternal MES function leads to germline degeneration and sterility. We report here that the MES complex is responsible for di- and trimethylation of histone H3 Lys27 (H3-K27) in the adult germline and in early embryos and that MES-dependent H3-K27 marks are concentrated on the X's. Another H3-K27 HMT functions in adult somatic cells, oocytes, and the PGCs of embryos. In PGCs, the MES complex may specifically convert dimethyl to trimethyl H3-K27. The HMT activity of the MES complex appears to be dependent on the SET domain of MES-2. MES-2 thus joins its orthologs Drosophila E(Z) and human EZH2 among SET domain proteins known to function as HMTs (reviewed in ). Methylation of histones is important for long-term epigenetic regulation of chromatin and plays a key role in diverse processes such as X inactivation and oncogenesis. Our results contribute to understanding the composition and roles of E(Z)/MES-2 complexes across species.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Mes-3 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/mes-2 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/mes-6 protein, C elegans
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0960-9822
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
21
|
pubmed:volume |
14
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1639-43
|
pubmed:dateRevised |
2009-10-1
|
pubmed:meshHeading |
pubmed-meshheading:15380065-Animals,
pubmed-meshheading:15380065-Blotting, Western,
pubmed-meshheading:15380065-Caenorhabditis elegans,
pubmed-meshheading:15380065-Caenorhabditis elegans Proteins,
pubmed-meshheading:15380065-Dosage Compensation, Genetic,
pubmed-meshheading:15380065-Fluorescent Antibody Technique,
pubmed-meshheading:15380065-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:15380065-Histones,
pubmed-meshheading:15380065-Immunoprecipitation,
pubmed-meshheading:15380065-Methylation,
pubmed-meshheading:15380065-Nuclear Proteins,
pubmed-meshheading:15380065-Protein Methyltransferases,
pubmed-meshheading:15380065-Protein Structure, Tertiary
|
pubmed:year |
2004
|
pubmed:articleTitle |
The MES-2/MES-3/MES-6 complex and regulation of histone H3 methylation in C. elegans.
|
pubmed:affiliation |
Department of Biology, Indiana University, Bloomington, IN 47405, USA.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|