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

Fingerprint

Cardiolipins
Die casting inserts
Membrane Potentials
Membranes
Peptides
Phosphatidylglycerols
Monolayers
Endopeptidase K
Mitochondrial Proteins
Mitochondrial Membranes
Trypsin
Peptide Hydrolases
Lipids

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes : Consequences for the action of a transmembrane potential. / Leenhouts, J. M.; Török, Z.; Mandieau, V.; Goormaghtigh, E.; De Kruijff, B.

In: FEBS Letters, Vol. 388, No. 1, 10.06.1996, p. 34-38.

Research output: Contribution to journalArticle

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