Takeda T, Ogino K, Tatebayashi K, Ikeda H, Masai H
Departments of Molecular and Developmental Biology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan.
Mol Biol Cell. 2001 May;12(5):1257-74. doi: 10.1091/mbc.12.5.1257.
Hsk1, Saccharomyces cerevisiae Cdc7-related kinase in Shizosaccharomyces pombe, is required for G1/S transition and its kinase activity is controlled by the regulatory subunit Dfp1/Him1. Analyses of a newly isolated temperature-sensitive mutant, hsk1-89, reveal that Hsk1 plays crucial roles in DNA replication checkpoint signaling and maintenance of proper chromatin structures during mitotic S phase through regulating the functions of Rad3 (ATM)-Cds1 and Rad21 (cohesin), respectively, in addition to expected essential roles for initiation of mitotic DNA replication through phosphorylating Cdc19 (Mcm2). Checkpoint defect in hsk1-89 is indicated by accumulation of cut cells at 30 degrees C. hsk1-89 displays synthetic lethality in combination with rad3 deletion, indicating that survival of hsk1-89 depends on Rad3-dependent checkpoint pathway. Cds1 kinase activation, which normally occurs in response to early S phase arrest by nucleotide deprivation, is largely impaired in hsk1-89. Furthermore, Cds1-dependent hyperphosphorylation of Dfp1 in response to hydroxyurea arrest is eliminated in hsk1-89, suggesting that sufficient activation of Hsk1-Dfp1 kinase is required for S phase entry and replication checkpoint signaling. hsk1-89 displays apparent defect in mitosis at 37 degrees C leading to accumulation of cells with near 2C DNA content and with aberrant nuclear structures. These phenotypes are similar to those of rad21-K1 and are significantly enhanced in a hsk1-89 rad21-K1 double mutant. Consistent with essential roles of Rad21 as a component for the cohesin complex, sister chromatid cohesion is partially impaired in hsk1-89, suggesting a possibility that infrequent origin firing of the mutant may affect the cohesin functions during S phase.
Hsk1是粟酒裂殖酵母中与酿酒酵母Cdc7相关的激酶,对于G1/S期转换是必需的,其激酶活性受调节亚基Dfp1/Him1的控制。对新分离的温度敏感突变体hsk1-89的分析表明,Hsk1除了通过磷酸化Cdc19(Mcm2)对有丝分裂DNA复制起始发挥预期的重要作用外,还分别通过调节Rad3(ATM)-Cds1和Rad21(黏连蛋白)的功能,在有丝分裂S期的DNA复制检查点信号传导和维持适当的染色质结构中发挥关键作用。hsk1-89中的检查点缺陷表现为在30℃时切割细胞的积累。hsk1-89与rad3缺失结合显示出合成致死性,表明hsk1-89的存活依赖于Rad3依赖性检查点途径。通常在核苷酸剥夺导致早期S期停滞时发生的Cds1激酶激活在hsk1-89中受到很大损害。此外,在hsk1-89中消除了对羟基脲停滞反应的Cds1依赖性Dfp1过度磷酸化,表明Hsk1-Dfp1激酶的充分激活是S期进入和复制检查点信号传导所必需的。hsk1-89在37℃时在有丝分裂中表现出明显缺陷,导致具有接近2C DNA含量和异常核结构的细胞积累。这些表型与rad21-K1的表型相似,并且在hsk1-89 rad21-K1双突变体中显著增强。与Rad21作为黏连蛋白复合物成分的重要作用一致,hsk1-89中姐妹染色单体黏连部分受损,这表明突变体不频繁的起始点激发可能会影响S期的黏连蛋白功能。