| pubmed-article:18245450 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18245450 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:18245450 | lifeskim:mentions | umls-concept:C1622022 | lld:lifeskim |
| pubmed-article:18245450 | lifeskim:mentions | umls-concept:C1155792 | lld:lifeskim |
| pubmed-article:18245450 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:18245450 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18245450 | pubmed:dateCreated | 2008-2-4 | lld:pubmed |
| pubmed-article:18245450 | pubmed:abstractText | S-phase cyclin-dependent kinase Cdc28-Clb5 (CDK-S) and Dbf4-dependent kinase Cdc7-Dbf4 (DDK) are highly conserved kinases well known for their roles in the initiation of DNA replication. CDK-S is also essential for initiation of meiotic recombination because it phosphorylates Ser30 of Mer2, a meiosis-specific double-strand break (DSB) protein. This work shows that the phosphorylation of Mer2 Ser30 by CDK-S primes Mer2 for subsequent phosphorylation by DDK on Ser29, creating a negatively charged "patch" necessary for DSB formation. CDK-S and DDK phosphorylation of Mer2 S30 and S29 can be bypassed by phosphomimetic amino acids, but break formation under these conditions is still dependent on DDK and CDK-S activity. Coordination between premeiotic S and DSB formation may be achieved by using CDK-S and DDK to initiate both processes. Many other proteins important for replication, recombination, repair, and chromosome segregation contain combination DDK/CDK sites, raising the possibility that this is a common regulatory mechanism. | lld:pubmed |
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| pubmed-article:18245450 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18245450 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18245450 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18245450 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18245450 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18245450 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:BoultonSimon... | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:ZhangChaoC | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:ShokatKevan... | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:FutcherBruceB | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:Hollingsworth... | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:WanLihongL | lld:pubmed |
| pubmed-article:18245450 | pubmed:author | pubmed-author:NiuHengyaoH | lld:pubmed |
| pubmed-article:18245450 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18245450 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18245450 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:18245450 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18245450 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18245450 | pubmed:pagination | 386-97 | lld:pubmed |
| pubmed-article:18245450 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:18245450 | pubmed:meshHeading | pubmed-meshheading:18245450... | lld:pubmed |
| pubmed-article:18245450 | pubmed:meshHeading | pubmed-meshheading:18245450... | lld:pubmed |
| pubmed-article:18245450 | pubmed:meshHeading | pubmed-meshheading:18245450... | lld:pubmed |
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| pubmed-article:18245450 | pubmed:meshHeading | pubmed-meshheading:18245450... | lld:pubmed |
