The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes: Consequences for the action of a transmembrane potential

J. M. Leenhouts, Z. Török, V. Mandieau, E. Goormaghtigh, B. De Kruijff

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The orientation of a mitochondrial presequence peptide, associated with anionic lipid-containing model membranes, was investigated. The peptide inserts with its N-terminal a-helical part into cardiolipin (CL) monolayers so that the N-terminal 14 residues are protected from proteinase K. In phosphatidylglycerol (PG) monolayers the inserted peptide was fully accessible to the protease. A consequence of the different orientations of the peptide was that membrane potential-dependent protection from trypsin was much faster for the peptide bound to PG-containing vesicles compared to CL-containing membranes, suggesting that in the mitochondrial protein import process other components of the import apparatus are involved in the efficient potential-driven translocation of presequences across the inner mitochondrial membrane.

Original languageEnglish
Pages (from-to)34-38
Number of pages5
JournalFEBS letters
Volume388
Issue number1
DOIs
Publication statusPublished - Jun 10 1996

Keywords

  • Amino acid sequence analysis
  • Membrane potential
  • Mitochondrial presequence
  • Monolayer insertion
  • Peptide topology

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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