Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

FEBS Lett. 1998 Nov 6;438(3):250-4. doi: 10.1016/s0014-5793(98)01310-6.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Adenosine Triphosphatases / chemistry*
  • Amino Acid Sequence
  • Animals
  • Bacteria / metabolism
  • Endopeptidase Clp
  • Escherichia coli Proteins
  • Fungal Proteins / chemistry*
  • Genes, Fungal
  • Mitochondria / metabolism*
  • Mitochondrial Proteins
  • Molecular Chaperones / analysis
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / genetics
  • Molecular Sequence Data
  • Nematoda
  • Plants / metabolism
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Escherichia coli Proteins
  • Fungal Proteins
  • Mcx1 protein, S cerevisiae
  • Mitochondrial Proteins
  • Molecular Chaperones
  • Saccharomyces cerevisiae Proteins
  • Endopeptidase Clp
  • Adenosine Triphosphatases
  • ClpX protein, E coli
  • ATPases Associated with Diverse Cellular Activities