Source:http://linkedlifedata.com/resource/pubmed/id/12400013
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2002-10-25
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pubmed:abstractText |
In response to replication block or DNA damage in S phase the DNA replication and DNA damage checkpoints are activated. The current model in human predicts, that a Rad17/Replication factor C (RF-C) complex might serve as a recruitment complex for the Rad9/Hus1/Rad1 complex to sites of replication block or DNA damage. In this study we have investigated the fate of the Rad17/RF-C complex after treatment of synchronized Hela cells with the replication inhibitor hydroxyurea. In hydroxyurea treated cells the RF-C p37 subunit became more resistant to extraction. Moreover, co-immunoprecipitation studies with extracts of hydroxyurea treated cells showed an interaction of RF-C p37 with Rad17 and of PCNA with Rad9 and RF-C p37. An enhanced colocalization of Rad17 and PCNA in late S phase after hydroxyurea treatment was observed. Our data suggested, that upon replication block a Rad17/RF-C complex is recruited to sites of DNA lesions in late S phase, binds the Rad9/Hus1/Rad1 complex and enables it to interact with PCNA. An interaction of Rad17/RF-C with PCNA appears to be mediated by the small RF-C p37 subunit, suggesting that PCNA might provide communication between replication checkpoint control and DNA replication and repair.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-Nitroquinoline-1-oxide,
http://linkedlifedata.com/resource/pubmed/chemical/4-nitroquinolone-1-oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyurea,
http://linkedlifedata.com/resource/pubmed/chemical/Proliferating Cell Nuclear Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Quinolones,
http://linkedlifedata.com/resource/pubmed/chemical/RFC4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Rad17 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Replication Protein C
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7710-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12400013-4-Nitroquinoline-1-oxide,
pubmed-meshheading:12400013-Cell Cycle,
pubmed-meshheading:12400013-Cell Cycle Proteins,
pubmed-meshheading:12400013-Cell Nucleus,
pubmed-meshheading:12400013-DNA Replication,
pubmed-meshheading:12400013-DNA-Binding Proteins,
pubmed-meshheading:12400013-HeLa Cells,
pubmed-meshheading:12400013-Humans,
pubmed-meshheading:12400013-Hydroxyurea,
pubmed-meshheading:12400013-Proliferating Cell Nuclear Antigen,
pubmed-meshheading:12400013-Quinolones,
pubmed-meshheading:12400013-Replication Protein C,
pubmed-meshheading:12400013-S Phase
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pubmed:year |
2002
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pubmed:articleTitle |
Colocalization of human Rad17 and PCNA in late S phase of the cell cycle upon replication block.
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pubmed:affiliation |
Institute of Veterinary Biochemistry and Molecular Biology, University Zürich-Irchel, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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