Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae
Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae
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DOI：
10.1016/s0014-5793(98)01310-6
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发表时间：
1998-11-06
期刊：
影响因子：
3.5
通讯作者：
Langer, T
中科院分区：
文献类型：
--
作者：
van Dyck, L;Dembowski, M;Langer, T
Hsp 100/C1 p-家族的分子伴侣形成ATP依赖性C1 p蛋白酶的调节亚基，并在细胞耐热性中发挥关键作用。我们在酿酒酵母中发现了一种C1 p样蛋白Mcx 1 p，它与细菌、植物和线虫中的C1 pX蛋白有30%的序列同源性，Mcx 1 p定位于线粒体的基质空间，并与内膜外周相连。E. coli C1 pP蛋白酶在筛选酵母基因组时未被鉴定。因此，我们建议，Mcx 1 p代表一种新的非蛋白水解功能的线粒体分子伴侣。(C)1998年欧洲生物化学学会联合会。
Members of the Hsp100/C1p-family of molecular chaperones form regulatory subunits of ATP-dependent C1p proteases and fulfill crucial roles for cellular thermotolerance. We have identified a C1p-like protein in Saccharomyces cerevisiae, Mcx1p, which shares approximately 30% sequence identity with C1pX-proteins in bacteria, plants and nematodes, Mcx1p localizes to the matrix space of mitochondria and is peripherally associated with the inner membrane. A homologue of E. coli C1pP protease was not identified when screening the yeast genome. We therefore propose that Mcx1p represents a novel molecular chaperone of mitochondria with non-proteolytic function. (C) 1998 Federation of European Biochemical Societies.