DC Field | Value | Language |
---|---|---|
dc.contributor.author | Tak Y.-S. | ko |
dc.contributor.author | Tanaka Y. | ko |
dc.contributor.author | Endo S. | ko |
dc.contributor.author | Kamimura Y. | ko |
dc.contributor.author | Araki H. | ko |
dc.date.accessioned | 2013-03-06T06:40:09Z | - |
dc.date.available | 2013-03-06T06:40:09Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | EMBO JOURNAL, v.25, no.9, pp.1987 - 1996 | - |
dc.identifier.issn | 0261-4189 | - |
dc.identifier.uri | http://hdl.handle.net/10203/86156 | - |
dc.description.abstract | Phosphorylation often regulates protein-protein interactions to control biological reactions. The Sld2 and Dpb11 proteins of budding yeast form a phosphorylation-dependent complex that is essential for chromosomal DNA replication. The Sld2 protein has a cluster of 11 cyclin-dependent kinase (CDK) phosphorylation motifs (Ser/Thr-Pro), six of which match the canonical sequences Ser/Thr-Pro-X-Lys/Arg, Lys/Arg-Ser/Thr-Pro and Ser/Thr-Pro-Lys/Arg. Simultaneous alanine substitution for serine or threonine in all the canonical CDK-phosphorylation motifs severely reduces complex formation between Sld2 and Dpb11, and inhibits DNA replication. Here we show that phosphorylation of these canonical motifs does not play a direct role in complex formation, but rather regulates phosphorylation of another residue, Thr84. This constitutes a non-canonical CDK-phosphorylation motif within a 28-amino-acid sequence that is responsible, after phosphorylation, for binding of Sld2-Dpb11. We further suggest that CDK-catalysed phosphorylation of sites other than Thr84 renders Thr84 accessible to CDK. Finally, we argue that this novel mechanism sets a threshold of CDK activity for formation of the essential Sld2 to Dpb11 complex and therefore prevents premature DNA replication. | - |
dc.language | English | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.subject | CYCLIN-DEPENDENT KINASES | - |
dc.subject | SACCHAROMYCES-CEREVISIAE | - |
dc.subject | CHROMOSOMAL DNA | - |
dc.subject | BUDDING YEAST | - |
dc.subject | CELL-CYCLE | - |
dc.subject | MULTISITE PHOSPHORYLATION | - |
dc.subject | 2-HYBRID SYSTEM | - |
dc.subject | RE-REPLICATION | - |
dc.subject | FISSION YEAST | - |
dc.subject | BRCT REPEATS | - |
dc.title | A CDK-catalysed regulatory phosphorylation for formation of the DNA replication complex Sld2-Dpb11 | - |
dc.type | Article | - |
dc.identifier.wosid | 000237589900019 | - |
dc.identifier.scopusid | 2-s2.0-33646578509 | - |
dc.type.rims | ART | - |
dc.citation.volume | 25 | - |
dc.citation.issue | 9 | - |
dc.citation.beginningpage | 1987 | - |
dc.citation.endingpage | 1996 | - |
dc.citation.publicationname | EMBO JOURNAL | - |
dc.identifier.doi | 10.1038/sj.emboj.7601075 | - |
dc.contributor.localauthor | Tak Y.-S. | - |
dc.contributor.nonIdAuthor | Tanaka Y. | - |
dc.contributor.nonIdAuthor | Endo S. | - |
dc.contributor.nonIdAuthor | Kamimura Y. | - |
dc.contributor.nonIdAuthor | Araki H. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | BRCT | - |
dc.subject.keywordAuthor | CDK | - |
dc.subject.keywordAuthor | DNA replication | - |
dc.subject.keywordAuthor | phosphorylation | - |
dc.subject.keywordAuthor | S phase | - |
dc.subject.keywordPlus | CYCLIN-DEPENDENT KINASES | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | CHROMOSOMAL DNA | - |
dc.subject.keywordPlus | BUDDING YEAST | - |
dc.subject.keywordPlus | CELL-CYCLE | - |
dc.subject.keywordPlus | MULTISITE PHOSPHORYLATION | - |
dc.subject.keywordPlus | 2-HYBRID SYSTEM | - |
dc.subject.keywordPlus | RE-REPLICATION | - |
dc.subject.keywordPlus | FISSION YEAST | - |
dc.subject.keywordPlus | BRCT REPEATS | - |
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