Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-10-31
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CAF1 protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/E(z) protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Polycomb protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma-Binding Protein 4, http://linkedlifedata.com/resource/pubmed/chemical/Su(z)12 protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Ubx protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/esc protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-208
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12408864-Animals, pubmed-meshheading:12408864-Chromosomal Proteins, Non-Histone, pubmed-meshheading:12408864-DNA-Binding Proteins, pubmed-meshheading:12408864-Drosophila, pubmed-meshheading:12408864-Drosophila Proteins, pubmed-meshheading:12408864-Gene Silencing, pubmed-meshheading:12408864-Histone-Lysine N-Methyltransferase, pubmed-meshheading:12408864-Homeodomain Proteins, pubmed-meshheading:12408864-Insect Proteins, pubmed-meshheading:12408864-Lysine, pubmed-meshheading:12408864-Methyltransferases, pubmed-meshheading:12408864-Molecular Chaperones, pubmed-meshheading:12408864-Nuclear Proteins, pubmed-meshheading:12408864-Protein Methyltransferases, pubmed-meshheading:12408864-Recombination, Genetic, pubmed-meshheading:12408864-Repressor Proteins, pubmed-meshheading:12408864-Retinoblastoma-Binding Protein 4, pubmed-meshheading:12408864-Transcription Factors
pubmed:year
2002
pubmed:articleTitle
Histone methyltransferase activity of a Drosophila Polycomb group repressor complex.
pubmed:affiliation
EMBL, Gene Expression Programme, Meyerhofstr. 1, 69117 Heidelberg, Germany. mueller@embl-heidelberg.de
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't