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

FEBS Letters

Török, Z.²  de Kruijff, B.²  Goormaghtigh, E.¹  Leenhouts, J.M.²  Mandieau, V.¹ 

[1] Laboratoire de Chimie Physique des Macromolecules aux Interfaces, Université Libre de Bruxelles, Campus Plaine CP20612, B-1050 Bruxelles, Belgium;Department of Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

关键词: Mitochondrial presequence;    Peptide topology;    Monolayer insertion;    Amino acid sequence analysis;    Membrane potential;    ATR;    attenuated total reflection;    CL;    cardiolipin;    DOPC;    1;    2-dioleoyl-sn-glycero-3-phosphocholine;    DOPG;    1;    2-dioleoyl-sn-glycero-3-phosphoglycerol;    egg PC;    phosphatidylcholine from egg yolk;    EDTA;    (ethylenedinitrilo)tetraacetic acid;    FTIR;    Fourier transform infrared;    HEPES;    N-(2-hydroxyethyl)piperazine-N′-2-ethanesulfonic acid;    πi;    initial surface pressure;    Δπ;    surface pressure increase;    Δψ;    membrane potential;    LUVs;    large unilamellar vesicles;    p25;    peptide corresponding to the presequence of cytochrone oxidase subunit IV;    p25NBD;    p25 labeled with 7-nitro-2;    1;    3-benzoxadiazol-4-yl;    PK;    proteinase K;    POPG;    1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol;   

DOI  :  10.1016/0014-5793(96)00504-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown