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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2008-1-4
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pubmed:abstractText |
In yeast, global genome nucleotide-excision repair (GG-NER) requires a protein complex containing Rad7 and Rad16. Rad16 is a member of the switch/sucrose nonfermentable superfamily, and it is presumed that chromatin remodelling is its primary function during repair. We show that RAD16 is required for ultraviolet-dependent hyperacetylation of histone H3 (Lys 9 and Lys 14) at the MFA2 promoter and throughout the genome. The yeast repressor complex Ssn6-Tup1 represses many genes including MFA2. TUP1 deletion results in constitutive hyperacetylation of histone H3, nucleosome disruption and derepression of gene transcription in Tup1-regulated genes. GG-NER in the MFA2 promoter proceeds more rapidly in tup1Delta alpha-cells compared with wild type, even when transcription is inhibited. We show that elevated histone H3 acetylation levels in the MFA2 promoter in tup1Delta alpha-cells result in Rad7- and Rad16-independent GG-NER, and that Rad16 mediates the ultraviolet-induced acetylation of histone H3, necessary for efficient GG-NER.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-10466730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-10601031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-11030336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-11056171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-11116189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-11163188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-11433040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-11866513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-12123289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-14734564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-1508678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-15177043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-15939881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-16675952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-16936817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-16936822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-17013386,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-1739976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-7651832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-7926740,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-8065346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-8552076,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-9096229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-9268290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-9792654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18007656-9813069
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/MFA2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pheromones,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidine Dimers,
http://linkedlifedata.com/resource/pubmed/chemical/RAD16 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD7 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TUP1 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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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 |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
97-102
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18007656-Acetylation,
pubmed-meshheading:18007656-Adenosine Triphosphatases,
pubmed-meshheading:18007656-DNA Repair,
pubmed-meshheading:18007656-DNA-Binding Proteins,
pubmed-meshheading:18007656-Gene Deletion,
pubmed-meshheading:18007656-Gene Expression Regulation, Fungal,
pubmed-meshheading:18007656-Genes, Fungal,
pubmed-meshheading:18007656-Genome, Fungal,
pubmed-meshheading:18007656-Histones,
pubmed-meshheading:18007656-Lipoproteins,
pubmed-meshheading:18007656-Nuclear Proteins,
pubmed-meshheading:18007656-Pheromones,
pubmed-meshheading:18007656-Pyrimidine Dimers,
pubmed-meshheading:18007656-Repressor Proteins,
pubmed-meshheading:18007656-Saccharomyces cerevisiae,
pubmed-meshheading:18007656-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:18007656-Sequence Analysis, DNA,
pubmed-meshheading:18007656-Transcription, Genetic,
pubmed-meshheading:18007656-Ultraviolet Rays
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pubmed:year |
2008
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pubmed:articleTitle |
Saccharomyces cerevisiae Rad16 mediates ultraviolet-dependent histone H3 acetylation required for efficient global genome nucleotide-excision repair.
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pubmed:affiliation |
Department of Pathology, School of Medicine, Cardiff University, Heath Park, Cardiff, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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