| pubmed-article:12408864 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12408864 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:12408864 | lifeskim:mentions | umls-concept:C1336789 | lld:lifeskim |
| pubmed-article:12408864 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:12408864 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:12408864 | lifeskim:mentions | umls-concept:C1152280 | lld:lifeskim |
| pubmed-article:12408864 | lifeskim:mentions | umls-concept:C0083956 | lld:lifeskim |
| pubmed-article:12408864 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12408864 | pubmed:dateCreated | 2002-10-31 | lld:pubmed |
| pubmed-article:12408864 | pubmed:abstractText | Polycomb group (PcG) proteins maintain transcriptional repression during development, likely by creating repressive chromatin states. The Extra Sex Combs (ESC) and Enhancer of Zeste [E(Z)] proteins are partners in an essential PcG complex, but its full composition and biochemical activities are not known. A SET domain in E(Z) suggests this complex might methylate histones. We purified an ESC-E(Z) complex from Drosophila embryos and found four major subunits: ESC, E(Z), NURF-55, and the PcG repressor, SU(Z)12. A recombinant complex reconstituted from these four subunits methylates lysine-27 of histone H3. Mutations in the E(Z) SET domain disrupt methyltransferase activity in vitro and HOX gene repression in vivo. These results identify E(Z) as a PcG protein with enzymatic activity and implicate histone methylation in PcG-mediated silencing. | lld:pubmed |
| pubmed-article:12408864 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12408864 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12408864 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12408864 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:12408864 | pubmed:author | pubmed-author:KingstonRober... | lld:pubmed |
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| pubmed-article:12408864 | pubmed:author | pubmed-author:SimonJeffrey... | lld:pubmed |
| pubmed-article:12408864 | pubmed:author | pubmed-author:HartCraig MCM | lld:pubmed |
| pubmed-article:12408864 | pubmed:author | pubmed-author:FrancisNicole... | lld:pubmed |
| pubmed-article:12408864 | pubmed:author | pubmed-author:MüllerJürgJ | lld:pubmed |
| pubmed-article:12408864 | pubmed:author | pubmed-author:VargasMarcus... | lld:pubmed |
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| pubmed-article:12408864 | pubmed:author | pubmed-author:WildBrigitteB | lld:pubmed |
| pubmed-article:12408864 | pubmed:author | pubmed-author:MillerEllen... | lld:pubmed |
| pubmed-article:12408864 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12408864 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:12408864 | pubmed:volume | 111 | lld:pubmed |
| pubmed-article:12408864 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12408864 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12408864 | pubmed:pagination | 197-208 | lld:pubmed |
| pubmed-article:12408864 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12408864 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12408864 | pubmed:articleTitle | Histone methyltransferase activity of a Drosophila Polycomb group repressor complex. | lld:pubmed |
| pubmed-article:12408864 | pubmed:affiliation | EMBL, Gene Expression Programme, Meyerhofstr. 1, 69117 Heidelberg, Germany. mueller@embl-heidelberg.de | lld:pubmed |
| pubmed-article:12408864 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12408864 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12408864 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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