DEFECTIVE MITOSIS DUE TO A MUTATION IN THE GENE FOR A FISSION YEAST 26S PROTEASE SUBUNIT
DEFECTIVE MITOSIS DUE TO A MUTATION IN THE GENE FOR A FISSION YEAST 26S PROTEASE SUBUNIT
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DOI：
10.1038/366355a0
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发表时间：
1993-11-25
期刊：
影响因子：
64.8
通讯作者：
HASTIE, ND
中科院分区：
文献类型：
--
作者：
GORDON, C;MCGURK, G;HASTIE, ND
我们在裂殖酵母粟酒裂殖酵母中分离到一个染色体分离缺陷的突变体mts 2。预测的氨基酸序列的克隆mts 2+基因产物是75%相同的人26 S ATP/泛素依赖性蛋白酶1的S4亚基。从S.粟酒裂殖酵母表达质粒可拯救S. pombe mts 2基因破坏。这两个观察结果表明，mts 2+基因是S.粟酒裂殖子同源的人S4亚单位。此外，我们提供了遗传证据的物理相互作用之间的S4和相关的S7亚基的26 S多蛋白蛋白酶。我们发现，在限制性温度下，多聚泛素结合蛋白在mts 2突变体中积累，表明该突变体在泛素依赖的蛋白水解途径中存在体内缺陷。最后，mts 2突变体的表型表明，蛋白质降解的26 S蛋白酶是必不可少的，而不是进入有丝分裂，但完成。
WE have isolated a mutant, mts2, in the fission yeast Schizosaccharomyces pombe which is defective in chromosome segregation. The predicted amino-acid sequence of the cloned mts2+ gene product is 75% identical to the S4 subunit of the human 26S ATP/ubiquitin-dependent protease1. The human S4 subunit complementary DNA expressed from an S. pombe expression plasmid can rescue an S. pombe mts2 gene disruption. Both observations demonstrate that the mts2+ gene is the S. pombe homologue of the human S4 subunit. In addition, we provide genetic evidence for a physical interaction between the S4 and the related S7 subunit in the 26S multiprotein protease. We show that polyubiquitin-conjugated proteins accumulate in the mts2 mutant at the restrictive temperature, demonstrating that the mutant has an in vivo defect in the ubiquitin-dependent proteolysis pathway. Finally, the phenotype for the mts2 mutant indicates that protein degradation by the 26S protease is essential not for entry into but for the completion of mitosis.