pubmed-article:21209461 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C0090388 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
pubmed-article:21209461 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
pubmed-article:21209461 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:21209461 | pubmed:dateCreated | 2011-4-1 | lld:pubmed |
pubmed-article:21209461 | pubmed:abstractText | CAF-1 is essential in human cells for the de novo deposition of histones H3 and H4 at the DNA replication fork. Depletion of CAF-1 from various cell lines causes replication fork arrest, activation of the intra-S phase checkpoint, and global defects in chromatin structure. CAF-1 is also involved in coordinating inheritance of states of gene expression and in chromatin assembly following DNA repair. In this study, we generated cell lines expressing RNAi-resistant versions of CAF-1 and showed that the N-terminal 296 amino acids are dispensable for essential CAF-1 function in vivo. N-terminally truncated CAF-1 p150 was deficient in proliferating cell nuclear antigen (PCNA) binding, reinforcing the existence of two PCNA binding sites in human CAF-1, but the defect in PCNA binding had no effect on the recruitment of CAF-1 to chromatin after DNA damage or to resistance to DNA-damaging agents. Tandem affinity purification of CAF-1-interacting proteins under mild conditions revealed that CAF-1 was directly associated with the KU70/80 complex, part of the DNA-dependent protein kinase, and the phosphoserine/threonine-binding protein 14-3-3 ?. CAF-1 was a substrate for DNA-dependent protein kinase, and the 14-3-3 interaction in vitro is dependent on DNA-dependent protein kinase phosphorylation. These results highlight that CAF-1 has prominent interactions with the DNA repair machinery but that the N terminus is dispensable for the role of CAF-1 in DNA replication- and repair-coupled chromatin assembly. | lld:pubmed |
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pubmed-article:21209461 | pubmed:language | eng | lld:pubmed |
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pubmed-article:21209461 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:21209461 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21209461 | pubmed:month | Mar | lld:pubmed |
pubmed-article:21209461 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:21209461 | pubmed:author | pubmed-author:StillmanBruce... | lld:pubmed |
pubmed-article:21209461 | pubmed:author | pubmed-author:HoekMaartenM | lld:pubmed |
pubmed-article:21209461 | pubmed:author | pubmed-author:MyersMichael... | lld:pubmed |
pubmed-article:21209461 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21209461 | pubmed:day | 25 | lld:pubmed |
pubmed-article:21209461 | pubmed:volume | 286 | lld:pubmed |
pubmed-article:21209461 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21209461 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21209461 | pubmed:pagination | 10876-87 | lld:pubmed |
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pubmed-article:21209461 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21209461 | pubmed:articleTitle | An analysis of CAF-1-interacting proteins reveals dynamic and direct interactions with the KU complex and 14-3-3 proteins. | lld:pubmed |
pubmed-article:21209461 | pubmed:affiliation | Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA. | lld:pubmed |
pubmed-article:21209461 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21209461 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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