pubmed-article:10913172 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C0007586 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C1419232 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C1419352 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C1751194 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:10913172 | lifeskim:mentions | umls-concept:C0392337 | lld:lifeskim |
pubmed-article:10913172 | pubmed:issue | 16 | lld:pubmed |
pubmed-article:10913172 | pubmed:dateCreated | 2000-8-28 | lld:pubmed |
pubmed-article:10913172 | pubmed:abstractText | RAD24 and RFC5 are required for DNA damage checkpoint control in the budding yeast Saccharomyces cerevisiae. Rad24 is structurally related to replication factor C (RFC) subunits and associates with RFC subunits Rfc2, Rfc3, Rfc4, and Rfc5. rad24Delta mutants are defective in all the G(1)-, S-, and G(2)/M-phase DNA damage checkpoints, whereas the rfc5-1 mutant is impaired only in the S-phase DNA damage checkpoint. Both the RFC subunits and Rad24 contain a consensus sequence for nucleoside triphosphate (NTP) binding. To determine whether the NTP-binding motif is important for Rad24 function, we mutated the conserved lysine(115) residue in this motif. The rad24-K115E mutation, which changes lysine to glutamate, confers a complete loss-of-function phenotype, while the rad24-K115R mutation, which changes lysine to arginine, shows no apparent phenotype. Although neither rfc5-1 nor rad24-K115R single mutants are defective in the G(1)- and G(2)/M-phase DNA damage checkpoints, rfc5-1 rad24-K115R double mutants become defective in these checkpoints. Coimmunoprecipitation experiments revealed that Rad24(K115R) fails to interact with the RFC proteins in rfc5-1 mutants. Together, these results indicate that RFC5, like RAD24, functions in all the G(1)-, S- and G(2)/M-phase DNA damage checkpoints and suggest that the interaction of Rad24 with the RFC proteins is essential for DNA damage checkpoint control. | lld:pubmed |
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pubmed-article:10913172 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10913172 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10913172 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10913172 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10913172 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:10913172 | pubmed:author | pubmed-author:KondoTT | lld:pubmed |
pubmed-article:10913172 | pubmed:author | pubmed-author:ShimomuraTT | lld:pubmed |
pubmed-article:10913172 | pubmed:author | pubmed-author:MatsumotoKK | lld:pubmed |
pubmed-article:10913172 | pubmed:author | pubmed-author:SugimotoKK | lld:pubmed |
pubmed-article:10913172 | pubmed:author | pubmed-author:NaikiTT | lld:pubmed |
pubmed-article:10913172 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10913172 | pubmed:volume | 20 | lld:pubmed |
pubmed-article:10913172 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10913172 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10913172 | pubmed:pagination | 5888-96 | lld:pubmed |
pubmed-article:10913172 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10913172 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10913172 | pubmed:articleTitle | Rfc5, in cooperation with rad24, controls DNA damage checkpoints throughout the cell cycle in Saccharomyces cerevisiae. | lld:pubmed |
pubmed-article:10913172 | pubmed:affiliation | Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-0814, Japan. | lld:pubmed |
pubmed-article:10913172 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10913172 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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