Mutations in a 19-Amino-Acid Hydrophobic Region of the Yeast Cytochrome c1 Presequence Prevent Sorting to the Mitochondrial Intermembrane Space

Robert E. Jensen, Susan Schmidt, Robert J. Mark

Research output: Contribution to journalArticle

Abstract

Most mitochondrial proteins destined for the intermembrane space (IMS) carry in their presequence information for localization to the IMS in addition to information for their import. By selecting for mutants in the yeast Saccharomyces cerevisiae that mislocalize an IMS-targeted fusion protein, we identified mutations in the IMS sorting signal of the cytochrome c1 protein. Amino acid substitutions or deletions in a stretch of 19 hydrophobic amino acids of the cytochrome c1 presequence resulted in accumulation of the intermediate form of the cytochrome c1 protein in the matrix. In some cases, the accumulated intermediate appeared to be slowly exported from the matrix, across the inner membrane to the IMS. Our results support the hypothesis that the cytochrome c1 precursor is normally imported completely into the matrix and then exported to the IMS.

Original languageEnglish (US)
Pages (from-to)4677-4686
Number of pages10
JournalMolecular and cellular biology
Volume12
Issue number10
DOIs
StatePublished - Oct 1992

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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