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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5514
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pubmed:dateCreated |
2001-4-9
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pubmed:abstractText |
The assembly of higher order chromatin structures has been linked to the covalent modifications of histone tails. We provide in vivo evidence that lysine 9 of histone H3 (H3 Lys9) is preferentially methylated by the Clr4 protein at heterochromatin-associated regions in fission yeast. Both the conserved chromo- and SET domains of Clr4 are required for H3 Lys9 methylation in vivo. Localization of Swi6, a homolog of Drosophila HP1, to heterochomatic regions is dependent on H3 Lys9 methylation. Moreover, an H3-specific deacetylase Clr3 and a beta-propeller domain protein Rik1 are required for H3 Lys9 methylation by Clr4 and Swi6 localization. These data define a conserved pathway wherein sequential histone modifications establish a "histone code" essential for the epigenetic inheritance of heterochromatin assembly.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Clr3 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heterochromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
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/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SWI6 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/clr4 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0036-8075
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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 |
292
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
110-3
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11283354-Acetylation,
pubmed-meshheading:11283354-Cell Cycle Proteins,
pubmed-meshheading:11283354-Centromere,
pubmed-meshheading:11283354-Chromosomes, Fungal,
pubmed-meshheading:11283354-Fungal Proteins,
pubmed-meshheading:11283354-Gene Silencing,
pubmed-meshheading:11283354-Genes, Fungal,
pubmed-meshheading:11283354-Heterochromatin,
pubmed-meshheading:11283354-Histone Deacetylases,
pubmed-meshheading:11283354-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:11283354-Histones,
pubmed-meshheading:11283354-Lysine,
pubmed-meshheading:11283354-Methylation,
pubmed-meshheading:11283354-Methyltransferases,
pubmed-meshheading:11283354-Mutation,
pubmed-meshheading:11283354-Protein Methyltransferases,
pubmed-meshheading:11283354-Protein Structure, Tertiary,
pubmed-meshheading:11283354-Recombinant Proteins,
pubmed-meshheading:11283354-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11283354-Schizosaccharomyces,
pubmed-meshheading:11283354-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:11283354-Transcription Factors
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pubmed:year |
2001
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pubmed:articleTitle |
Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly.
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pubmed:affiliation |
Cold Spring Harbor Laboratory, Post Office Box 100, Cold Spring Harbor, NY 11724, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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