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The N‐terminal half of a mitochondrial presequence peptide inserts into cardiolipin‐containing membranes Consequences for the action of a transmembrane potential
Author(s) -
Leenhouts J.M.,
Török Z.,
Mandieau V.,
Goormaghtigh E.,
de Kruijff B.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00504-2
Subject(s) - cardiolipin , peptide , transmembrane protein , membrane , inner mitochondrial membrane , membrane potential , chemistry , terminal (telecommunication) , mitochondrial membrane transport protein , mitochondrion , biochemistry , action (physics) , biophysics , biology , phospholipid , telecommunications , physics , quantum mechanics , computer science , receptor
The orientation of a mitochondrial presequence peptide, associated with anionic lipid‐containing model membranes, was investigated. The peptide inserts with its N‐terminal α‐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.