| Literature DB >> 21487389 |
Tamon Tanaka1, Toshiko Umemori, Shizuko Endo, Sachiko Muramatsu, Masato Kanemaki, Yoichiro Kamimura, Chikashi Obuse, Hiroyuki Araki.
Abstract
Genetic screening of yeast for sld (synthetic lethality with dpb11) mutations has identified replication proteins, including Sld2, -3, and -5, and clarified the molecular mechanisms underlying eukaryotic chromosomal DNA replication. Here, we report a new replication protein, Sld7, identified by rescreening of sld mutations. Throughout the cell cycle, Sld7 forms a complex with Sld3, which associates with replication origins in a complex with Cdc45, binds to Dpb11 when phosphorylated by cyclin-dependent kinase, and dissociates from origins once DNA replication starts. However, Sld7 does not move with the replication fork. Sld7 binds to the nonessential N-terminal portion of Sld3 and reduces its affinity for Cdc45, a component of the replication fork. Although Sld7 is not essential for cell growth, its absence reduces the level of cellular Sld3, delays the dissociation from origins of GINS, a component of the replication fork, and slows S-phase progression. These results suggest that Sld7 is required for the proper function of Sld3 at the initiation of DNA replication.Entities:
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Year: 2011 PMID: 21487389 PMCID: PMC3098486 DOI: 10.1038/emboj.2011.115
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598