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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase.
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The Cdc23 (Mcm10) protein is required for the phosphorylation of minichromosome maintenance complex by the Dfp1-Hsk1 kinase.

机译：Cdc23（Mcm10）蛋白是Dfp1-Hsk1激酶使微染色体维持复合物磷酸化所必需的。

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摘要

Previous studies in Saccharomyces cerevisiae have defined an essential role for the Dbf4-Cdc7 kinase complex in the initiation of DNA replication presumably by phosphorylation of target proteins, such as the minichromosome maintenance (Mcm) complex. We have examined the phosphorylation of the Mcm complex by the Dfp1-Hsk1 kinase, the Schizosaccharomyces pombe homologue of Dbf4-Cdc7. In vitro, the purified Dfp1-Hsk1 kinase efficiently phosphorylated Mcm2p. In contrast, Mcm2p, present in the six-subunit Mcm complex, was a poor substrate of this kinase and required Cdc23p (homologue of Mcm10p) for efficient phosphorylation. In the presence of Cdc23p, Dfp1-Hsk1 phosphorylated the Mcm2p and Mcm4p subunits of the Mcm complex. Cdc23p interacted with both the Mcm complex and Dfp1-Hsk1 by selectively binding to the Mcm467 subunits and Dfp1p, respectively. The N terminus of Cdc23p was found to interact directly with Dfp1-Hsk1 and was essential for phosphorylation of the Mcm complex. Truncated derivatives of Cdc23p that complemented the temperature-sensitive phenotype of cdc23 mutant cells also stimulated the phosphorylation of Mcm complex, implying that this activity might be a critical role of Cdc23p in vivo. These results suggest that Cdc23p participates in the activation of prereplicative complex by recruiting the Dfp1-Hsk1 kinase and stimulating the phosphorylation of the Mcm complex.
机译：先前在酿酒酵母中的研究已经确定了Dbf4-Cdc7激酶复合物在DNA复制起始中的重要作用，大概是通过靶蛋白（例如微染色体维持（Mcm）复合物）的磷酸化来实现的。我们已经检查了Dfp1-Hsk1激酶Dbf4-Cdc7的粟酒裂殖酵母同源物Mcm复合物的磷酸化。在体外，纯化的Dfp1-Hsk1激酶可有效地磷酸化Mcm2p。相反，存在于六个亚基Mcm复合物中的Mcm2p是该激酶的较弱底物，需要Cdc23p（Mcm10p的同源物）才能有效地进行磷酸化。在Cdc23p存在下，Dfp1-Hsk1磷酸化了Mcm复合体的Mcm2p和Mcm4p亚基。 Cdc23p通过分别绑定到Mcm467亚基和Dfp1p与Mcm复合物和Dfp1-Hsk1相互作用。发现Cdc23p的N末端直接与Dfp1-Hsk1相互作用，并且对于Mcm复合物的磷酸化至关重要。 Cdc23p的截短的衍生物补充了cdc23突变细胞的温度敏感性表型，也刺激了Mcm复合物的磷酸化，这暗示该活性可能是Cdc23p在体内的关键作用。这些结果表明，Cdc23p通过募集Dfp1-Hsk1激酶并刺激Mcm复合物的磷酸化参与复制前复合物的活化。

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