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首页> 外文期刊>Current Biology: CB >ATP Hydrolysis Is Required for Relocating Cohesin from Sites Occupied by Its Scc2/4 Loading Complex
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ATP Hydrolysis Is Required for Relocating Cohesin from Sites Occupied by Its Scc2/4 Loading Complex

机译：从其Scc2 / 4加载复合物占据的位点重新定位粘着蛋白需要ATP水解

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Background: The Cohesin complex that holds sister chromatins together until anaphase is comprised of three core subunits: Smc1 and Smc3, two long-rod-shaped proteins with an ABC-like ATPase head (nucleotide-binding domain [NBD]) and a dimerization domain linked by a 50 nm long intramolecular antiparallel coiled-coil, and Scc1, an alpha -kleisin subunit interconnecting the NBD domains of Smc1 and Smc3. Cohesin's stable association with chromosomes is thought to involve entrapment of chromatin fibers by its tripartite Smc1-Smc3-Scc1 ring via a poorly understood mechanism dependent on a separate Scc2/4 loading complex. A key issue concerns where entrapment initially takes place: at sites where cohesin is found stably associated or at distinct "loading" sites from which it translocates. Results: In this study, we find transition state mutant versions (Smc1E1158Q and SmcE1155Q) defective in disengagement of their nucleotide binding domains (NBDs), unlike functional cohesin, colocalize with Scc2/4 at core centromeres, sites that catalyze wild-type cohesin's recruitment to sequences 20 kb or more away. In addition to Scc2/4, the unstable association of transition state complexes with core centromeres requires Scc1's association with Smc1 and Smc3 NBDs, ATP-driven NBD engagement, cohesin's Scc3 subunit, and its hinge domain. Conclusion: We propose that cohesin's association with chromosomes is driven by two key events. NBD engagement driven by ATP binding produces an unstable association with specific loading sites like core centromeres, whereas subsequent ATP hydrolysis triggers DNA entrapment, which permits translocation along chromatin fibers.
机译：背景：将姐妹染色质保持在一起直至后期的粘着蛋白复合物由三个核心亚基组成：Smc1和Smc3，两个具有ABC样ATPase头的长杆状蛋白（核苷酸结合结构域[NBD]）和一个二聚化结构域由一个50 nm长的分子内反平行卷曲螺旋连接，以及Scc1，一个Scc1和Smc3的NBD结构域相互连接的α-kleisin亚基。 Cohesin与染色体的稳定关联被认为是通过依赖于一个单独的Scc2 / 4加载复合物的一个鲜为人知的机制，通过其三方Smc1-Smc3-Scc1环捕获了染色质纤维。一个关键问题涉及最初发生陷获的地方：在发现粘着蛋白稳定结合的位点或在其发生移位的不同“负载”位点。结果：在这项研究中，我们发现过渡状态突变体版本（Smc1E1158Q和SmcE1155Q）在其核苷酸结合结构域（NBD）的分离中存在缺陷，与功能性粘着蛋白不同，它们在核心着丝粒处与Scc2 / 4共定位，从而催化了野生型粘着蛋白的募集到20 kb或更远的距离。除Scc2 / 4外，过渡态复合物与核心着丝粒的不稳定关联还要求Scc1与Smc1和Smc3 NBD，ATP驱动的NBD参与，粘着蛋白的Scc3亚基及其铰链域关联。结论：我们认为粘着蛋白与染色体的关联是由两个关键事件驱动的。由ATP结合驱动的NBD参与会与特定的加载位点（如核心着丝粒）产生不稳定的关联，而随后的ATP水解则触发DNA截留，从而允许沿染色质纤维移位。

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