Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast
Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast
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DOI：
10.1016/s0092-8674(00)00130-6
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发表时间：
2000-10-27
期刊：
影响因子：
64.5
通讯作者：
Nasmyth, K
中科院分区：
文献类型：
--
作者：
Uhlmann, F;Wernic, D;Nasmyth, K
在真核细胞中，复制的DNA链保持物理连接，直到它们在分裂后期分离到细胞的两极。这种“姐妹染色单体凝聚”对于有丝分裂中期纺锤体上染色体的排列是必不可少的。凝聚力取决于多亚基凝聚素复合物，它可能形成连接姐妹篇的物理桥梁。蛋白水解切割的凝聚素的Scc1亚基在中期到后期的过渡是必不可少的姐妹染色单体分离，并依赖于一个保守的蛋白质称为分离。我们在这里表明，分离蛋白是一个半胱氨酸蛋白酶相关的半胱天冬酶，单独可以在体外切割Scc1。在中期阻滞细胞中Scc1的裂解足以触发姐妹染色单体的分离及其向相反细胞极的分离。
In eukaryotic cells, replicated DNA strands remain physically connected until their segregation to opposite poles of the cell during anaphase. This "sister chromatid cohesion" is essential for the alignment of chromosomes on the mitotic spindle during metaphase. Cohesion depends on the multisubunit cohesin complex, which possibly forms the physical bridges connecting sisters. Proteolytic cleavage of cohesin's Scc1 subunit at the metaphase to anaphase transition is essential for sister chromatid separation and depends on a conserved protein called separin. We show here that separin is a cysteine protease related to caspases that alone can cleave Scc1 in vitro. Cleavage of Scc1 in metaphase arrested cells is sufficient to trigger the separation of sister chromatids and their segregation to opposite cell poles.