Leenhouts J M, Török Z, Mandieau V, Goormaghtigh E, de Kruijff B
Department of Biochemistry of Membranes, Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, The Netherlands.
FEBS Lett. 1996 Jun 10;388(1):34-8. doi: 10.1016/0014-5793(96)00504-2.
The orientation of a mitochondrial-presequence peptide, associated with anionic lipid-containing model membranes, was investigated. The peptide inserts with its N-terminal alpha-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 membranes.
