Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

FEBS Letters

van Dyck, Luc¹  Neupert, Walter¹  Langer, Thomas¹  Dembowski, Markus¹ 

[1] Institut für Physiologische Chemie der Universität München, Goethestrasse 33, 80336 Munich, Germany

关键词: ClpX;    Hsp100;    Molecular chaperone;    Mitochondrion;   

DOI  :  10.1016/S0014-5793(98)01310-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Members of the Hsp100/Clp-family of molecular chaperones form regulatory subunits of ATP-dependent Clp proteases and fulfill crucial roles for cellular thermotolerance. We have identified a Clp-like protein in Saccharomyces cerevisiae, Mcx1p, which shares approximately 30% sequence identity with ClpX-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 ClpP 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.

【 授权许可】

Unknown