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rdf:type |
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lifeskim:mentions |
umls-concept:C0008546,
umls-concept:C0030685,
umls-concept:C0033414,
umls-concept:C0175721,
umls-concept:C0391871,
umls-concept:C0449432,
umls-concept:C0680255,
umls-concept:C1155874,
umls-concept:C1179435,
umls-concept:C1283071,
umls-concept:C1419245,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1622022,
umls-concept:C1705248,
umls-concept:C1883709,
umls-concept:C1963578
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pubmed:issue |
4
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pubmed:dateCreated |
2010-11-24
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pubmed:abstractText |
When inappropriate DNA structures arise, they are sensed by DNA structure-dependent checkpoint pathways and subsequently repaired. Recruitment of checkpoint proteins to such structures precedes recruitment of proteins involved in DNA metabolism. Thus, checkpoints can regulate DNA metabolism. We show that fission yeast Rad9, a 9-1-1 heterotrimeric checkpoint-clamp component, is phosphorylated by Hsk1(Cdc7), the Schizosaccharomyces pombe Dbf4-dependent kinase (DDK) homolog, in response to replication-induced DNA damage. Phosphorylation of Rad9 disrupts its interaction with replication protein A (RPA) and is dependent on 9-1-1 chromatin loading, the Rad9-associated protein Rad4/Cut5(TopBP1), and prior phosphorylation by Rad3(ATR). rad9 mutants defective in DDK phosphorylation show wild-type checkpoint responses but abnormal DNA repair protein foci and decreased viability after replication stress. We propose that Rad9 phosphorylation by DDK releases Rad9 from DNA damage sites to facilitate DNA repair.
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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/Camptothecin,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/DDK protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphothreonine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Replication Protein A,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rad9 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1097-4164
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
24
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
606-18
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pubmed:meshHeading |
pubmed-meshheading:21095590-Amino Acid Sequence,
pubmed-meshheading:21095590-Camptothecin,
pubmed-meshheading:21095590-Cell Cycle,
pubmed-meshheading:21095590-Cell Cycle Proteins,
pubmed-meshheading:21095590-Chromatin,
pubmed-meshheading:21095590-DNA Damage,
pubmed-meshheading:21095590-DNA Repair,
pubmed-meshheading:21095590-DNA Replication,
pubmed-meshheading:21095590-Enzyme Activation,
pubmed-meshheading:21095590-Kinetics,
pubmed-meshheading:21095590-Models, Biological,
pubmed-meshheading:21095590-Molecular Sequence Data,
pubmed-meshheading:21095590-Mutant Proteins,
pubmed-meshheading:21095590-Phosphorylation,
pubmed-meshheading:21095590-Phosphoserine,
pubmed-meshheading:21095590-Phosphothreonine,
pubmed-meshheading:21095590-Protein Binding,
pubmed-meshheading:21095590-Protein Transport,
pubmed-meshheading:21095590-Protein-Serine-Threonine Kinases,
pubmed-meshheading:21095590-Replication Protein A,
pubmed-meshheading:21095590-Schizosaccharomyces,
pubmed-meshheading:21095590-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:21095590-Solubility,
pubmed-meshheading:21095590-Subcellular Fractions,
pubmed-meshheading:21095590-Time Factors
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pubmed:year |
2010
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pubmed:articleTitle |
DDK phosphorylates checkpoint clamp component Rad9 and promotes its release from damaged chromatin.
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pubmed:affiliation |
Microbial Genetics Laboratory, Genetic Strains Research Center, National Institute of Genetics, 1111 Yata, Mishima, Shizuoka 411-8540, Japan. kfuruya@lab.nig.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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