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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-12-21
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pubmed:abstractText |
The postreplicative repair of double-strand breaks (DSBs) is thought to require sister chromatid cohesion, provided by the cohesin complex along the chromosome arms. A further specialized role for cohesin in DSB repair is suggested by its de novo recruitment to regions of DNA damage in mammals. Here, we show in budding yeast that a single DSB induces the formation of a approximately 100 kb cohesin domain around the lesion. Our analyses suggest that the primary DNA damage checkpoint kinases Mec1p and Tel1p phosphorylate histone H2AX to generate a large domain, which is permissive for cohesin binding. Cohesin binding to the phospho-H2AX domain is enabled by Mre11p, a component of a critical repair complex, and Scc2p, a component of the cohesin loading machinery that is necessary for sister chromatid cohesion. We also provide evidence that the DSB-induced cohesin domain functions in postreplicative repair.
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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/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/MRE11 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RAD53 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SCC2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SCC4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cohesins,
http://linkedlifedata.com/resource/pubmed/chemical/gamma-H2AX protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
991-1002
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15610741-Cell Cycle Proteins,
pubmed-meshheading:15610741-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:15610741-DNA,
pubmed-meshheading:15610741-DNA Damage,
pubmed-meshheading:15610741-DNA Repair,
pubmed-meshheading:15610741-Endodeoxyribonucleases,
pubmed-meshheading:15610741-Exodeoxyribonucleases,
pubmed-meshheading:15610741-Fungal Proteins,
pubmed-meshheading:15610741-Gene Conversion,
pubmed-meshheading:15610741-Histones,
pubmed-meshheading:15610741-Nuclear Proteins,
pubmed-meshheading:15610741-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15610741-Saccharomyces cerevisiae,
pubmed-meshheading:15610741-Saccharomyces cerevisiae Proteins
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pubmed:year |
2004
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pubmed:articleTitle |
DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Embryology, The Carnegie Institution of Washington, Baltimore, MD 21210, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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