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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-5-10
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pubmed:abstractText |
In Saccharomyces cerevisiae, known histone acetylation sites regulating gene activity are located in the N-terminal tails protruding from the nucleosome core. We report lysine 56 in histone H3 as a novel acetylation site that is located in the globular domain, where it extends toward the DNA major groove at the entry-exit points of the DNA superhelix as it wraps around the nucleosome. We show that K56 acetylation is enriched preferentially at certain active genes, such as those coding for histones. SPT10, a putative acetyltransferase, is required for cell cycle-specific K56 acetylation at histone genes. This allows recruitment of the nucleosome remodeling factor Snf5 and subsequent transcription. These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity.
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pubmed:grant |
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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/Acetyltransferases,
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/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/SMARCB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SNF5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SPT10 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SUC2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Fructofuranosidase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
121
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
375-85
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15882620-Acetylation,
pubmed-meshheading:15882620-Acetyltransferases,
pubmed-meshheading:15882620-Animals,
pubmed-meshheading:15882620-Cell Cycle,
pubmed-meshheading:15882620-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:15882620-DNA-Binding Proteins,
pubmed-meshheading:15882620-Drosophila melanogaster,
pubmed-meshheading:15882620-Gene Expression,
pubmed-meshheading:15882620-Gene Expression Profiling,
pubmed-meshheading:15882620-Gene Expression Regulation, Fungal,
pubmed-meshheading:15882620-HeLa Cells,
pubmed-meshheading:15882620-Histone Acetyltransferases,
pubmed-meshheading:15882620-Histones,
pubmed-meshheading:15882620-Humans,
pubmed-meshheading:15882620-Lysine,
pubmed-meshheading:15882620-Models, Molecular,
pubmed-meshheading:15882620-Mutation,
pubmed-meshheading:15882620-Protein Binding,
pubmed-meshheading:15882620-Saccharomyces cerevisiae,
pubmed-meshheading:15882620-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15882620-Transcription Factors,
pubmed-meshheading:15882620-beta-Fructofuranosidase
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pubmed:year |
2005
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pubmed:articleTitle |
Acetylation in histone H3 globular domain regulates gene expression in yeast.
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pubmed:affiliation |
Department of Biological Chemistry, Geffen School of Medicine at UCLA, and the Molecular Biology Institute, University of California-Los Angeles, Boyer Hall, Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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