Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

van Dyck, L.; Dembowski, M.; Neupert, W.; Langer, T.

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Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

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Langer, T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

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https://www.ncbi.nlm.nih.gov/pubmed/9827555
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Citation

van Dyck, L., Dembowski, M., Neupert, W., & Langer, T. (1998). Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae. FEBS Lett, 438(3), 250-4.

Cite as: https://hdl.handle.net/21.11116/0000-000B-6BEE-2

Abstract

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.