Molecular architecture of SMC proteins and the yeast cohesin complex
Molecular architecture of SMC proteins and the yeast cohesin complex
复制标题
DOI：
10.1016/s1097-2765(02)00515-4
复制
发表时间：
2002-04-01
期刊：
影响因子：
16
通讯作者：
Nasmyth, K
中科院分区：
文献类型：
--
作者：
Haering, CH;Löwe, J;Nasmyth, K
姐妹染色质由多亚基粘着蛋白配合物持有，其中包含两个SMC（SMC1和SMC3）和两个非SMC（SCC1和SCC3）蛋白。细菌SMC“铰链”区域的晶体结构以及酵母SMC1和SMC3蛋白上的EM研究和生化实验表明SMC精神素蛋白；单独折叠成棒状分子。 45 nm长的分子内盘绕线圈将铰链区域与含ATPase的“头”结构域分开。 SMC1和SMC3通过其铰链之间的异型相互作用相互结合，形成V形异二聚体。 V形二聚体的两个头部通过可裂解的SCC1亚基的不同末端连接。因此，粘着蛋白形成了大型蛋白质环，在DNA复制后可能会捕获姐妹染色单体。
Sister chromatids are held together by the multisubunit cohesin complex, which contains two SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3) proteins. The crystal structure of a bacterial SMC "hinge" region along with EM studies and biochemical experiments on yeast Smc1 and Smc3 proteins show that SMC protamers; fold up individually into rod-shaped molecules. A 45 nm long intramolecular coiled coil separates the hinge region from the ATPase-containing "head" domain. Smc1 and Smc3 bind to each other via heterotypic interactions between their hinges to form a V-shaped heterodimer. The two heads of the V-shaped dimer are connected by different ends of the cleavable Scc1 subunit. Cohesin therefore forms a large proteinaceous loop within which sister chromatids might be entrapped after DNA replication.