A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae.
A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae.
复制标题
在酿酒酵母中，泛素化在线粒体遗传中的作用。
DOI：
10.1083/jcb.145.6.1199
复制
发表时间：
1999-06-14
影响因子：
7.8
通讯作者：
Yaffe, M P
中科院分区：
文献类型：
--
作者：
Fisk, H A;Yaffe, M P
Smm1突变抑制由酿酒酵母中mdm1-252突变引起的线粒体分布和形态缺陷。只有smm1突变的细胞本身在不允许的温度下表现出对温度敏感的生长和异常的线粒体遗传和形态。Smm1定位于RSP5，这是一种编码一种重要的泛素蛋白连接酶的基因。Sm1缺陷被野生型泛素的过度表达所抑制，但不被突变泛素的过度表达所抑制，其中赖氨酸-63被精氨酸取代。此外，该突变泛素的过表达扰乱了野生型细胞中线粒体的分布和形态。定点突变研究表明，Rsp5p的泛素连接酶活性是其线粒体遗传功能所必需的。第二个突变smm2也抑制了mdm1-252缺陷，但没有导致线粒体分布和形态异常，定位于BUL1，编码与Rsp5p相互作用的蛋白质。这些结果表明，Rsp5p介导的蛋白质泛素化在线粒体遗传中起着重要作用，并揭示了蛋白质泛素化的一种新功能。
The smm1 mutation suppresses defects in mitochondrial distribution and morphology caused by the mdm1-252 mutation in the yeast Saccharomyces cerevisiae. Cells harboring only the smm1 mutation themselves display temperature-sensitive growth and aberrant mitochondrial inheritance and morphology at the nonpermissive temperature. smm1 maps to RSP5, a gene encoding an essential ubiquitin-protein ligase. The smm1 defects are suppressed by overexpression of wild-type ubiquitin but not by overexpression of mutant ubiquitin in which lysine-63 is replaced by arginine. Furthermore, overexpression of this mutant ubiquitin perturbs mitochondrial distribution and morphology in wild-type cells. Site-directed mutagenesis revealed that the ubiquitin ligase activity of Rsp5p is essential for its function in mitochondrial inheritance. A second mutation, smm2, which also suppressed mdm1-252 defects, but did not cause aberrant mitochondrial distribution and morphology, mapped to BUL1, encoding a protein interacting with Rsp5p. These results indicate that protein ubiquitination mediated by Rsp5p plays an essential role in mitochondrial inheritance, and reveal a novel function for protein ubiquitination.