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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2001-10-15
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pubmed:abstractText |
Modification of histones can have a dramatic impact on chromatin structure and function. Acetylation of lysines within the N-terminal tail of the histone octamer marks transcriptionally active regions of the genome whereas deacetylation seems to play a role in transcriptional silencing. Recently, the methylation of the histone tails has also been shown to be important for transcriptional regulation and chromosome structure. Here we show by immunoaffinity purification that two activities important for chromatin-mediated gene silencing, the histone methyltransferase SU(VAR)3-9 and the histone deacetylase HDAC1, associate in vivo. The two activities cooperate to methylate pre-acetylated histones. Both enzymes are modifiers of position effect variegation and interact genetically in flies. We suggest a model in which the concerted histone deacetylation and methylation by a SU(VAR)3-9/HDAC1-containing complex leads to a permanent silencing of transcription in particular areas of the genome.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10202156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10359792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10444591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10471500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10487762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10638745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10655219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10731132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-10949293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-11242053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-11242054,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-11280927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-11283354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-1365916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-2087785,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-6082620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-7915232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-8444870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-8955276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9149532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9150135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9428524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9468139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9487383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9620779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9620780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9674426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9695838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11571273-9780836
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HDAC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Salts
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1469-221X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
915-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11571273-Animals,
pubmed-meshheading:11571273-Blotting, Western,
pubmed-meshheading:11571273-Chromatin,
pubmed-meshheading:11571273-Drosophila,
pubmed-meshheading:11571273-Fungal Proteins,
pubmed-meshheading:11571273-Gene Silencing,
pubmed-meshheading:11571273-Genes, Dominant,
pubmed-meshheading:11571273-Genome,
pubmed-meshheading:11571273-Histone Deacetylase 1,
pubmed-meshheading:11571273-Histone Deacetylases,
pubmed-meshheading:11571273-Histones,
pubmed-meshheading:11571273-Lysine,
pubmed-meshheading:11571273-Methylation,
pubmed-meshheading:11571273-Methyltransferases,
pubmed-meshheading:11571273-Mutation,
pubmed-meshheading:11571273-Precipitin Tests,
pubmed-meshheading:11571273-Protein Binding,
pubmed-meshheading:11571273-Protein Structure, Tertiary,
pubmed-meshheading:11571273-Recombinant Proteins,
pubmed-meshheading:11571273-Salts,
pubmed-meshheading:11571273-Transcription, Genetic
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pubmed:year |
2001
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pubmed:articleTitle |
Physical and functional association of SU(VAR)3-9 and HDAC1 in Drosophila.
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pubmed:affiliation |
Adolf-Butenandt Institut, Molekularbiologie, Ludwig-Maximilians Universität, Schillerstrasse 44, D-80336 München, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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