Structure of the human GINS complex and its assembly and functional interface in replication initiation
Structure of the human GINS complex and its assembly and functional interface in replication initiation
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DOI：
10.1038/nsmb1231
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发表时间：
2007-05-01
影响因子：
16.8
通讯作者：
Hanaoka, Fumio
中科院分区：
文献类型：
--
作者：
Kamada, Katsuhiko;Kubota, Yumiko;Hanaoka, Fumio
真核GINS复合物对于DNA复制叉的建立和复制体的进展是必需的。我们报告的晶体结构的人GINS复合物。异源四聚体复合物采用包含两个异源二聚体的伪对称层状结构，产生四个亚基-亚基界面。异二聚体的亚基结构由两个交替的结构域组成。Sld 5和Psf 1亚基的C-末端结构域通过接头区域连接到核心复合物，并且Sld 5的C-末端结构域对于核心复合物组装是重要的。相反，Psf 1的C-末端结构域并不有助于复合物的稳定性，但对染色质结合和复制活性至关重要。这些数据表明，核心复合物确保了一个稳定的平台的C-末端结构域的Psf 1作为一个关键的相互作用界面的其他蛋白质在复制启动过程中。
The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process.