The full length of a mitochondrial presequence is required for efficient monolayer insertion and interbilayer contact formation

References

• Cullis P. R., De Kruijff B. 31P NMR studies of unsonicated aqueous dispersions of neutral and acidic phospholipids. Effects of phase transitions, p2H and divalent cations on the motion in the phosphate region of the polar head group. Biochimica et Biophysica Acta 1976; 436: 523–540
   Google Scholar
• Daum G. Lipids of mitochondria. Biochimica et Biophysica Acta 1985; 822: 1–42
   PubMed Web of Science ®Google Scholar
• De Kroon A. I. P. M., McConnell H. M. Kinetics and specificity of peptide-MHC Class II complex displacement reactions. Journal of Immunology 1994; 152: 609–619
   PubMed Web of Science ®Google Scholar
• De Kroon A. I. P.M., De Gier J., De Kruijff B. The effect of a membrane potential on the interaction of mastoparan X, a mitochondrial presequence, and several regulatory peptides with phospholipid vesicles. Biochimica et Biophysica Acta 1991; 1068: 111–124
   Google Scholar
• Demel R. A. Lipid-protein interactions in monomolecular layers. Current Topics in Membrane and Transport, A. Martonosi. Plenum, New York 1982; 159–164
   Google Scholar
• Endo T., Shimada I., Roise D., Inagaki F. N-terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: a proton nuclear magnetic resonance study. Journal of Biochemistry 1989; 106: 396–400
   Google Scholar
• Hope M. J., Bally M. B., Webb G., Cullis P. R. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochimica et Biophysica Acta 1985; 812: 55–65
   PubMed Web of Science ®Google Scholar
• Hurt E. C., Pesold-Hurt B., Suda K., Oppliger W., Schatz G. The first twelve amino acids (less than half of the presequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. EMBO Journal 1985; 4: 2061–2068
   PubMed Web of Science ®Google Scholar
• Hurt E. C., Allison D. S., Müller U., Schatz G. Aminoterminal deletions in the presequence of an imported mitochondrial protein block the targeting function and proteolytic cleavage of the presequence at the carboxy terminus. Journal of Biological Chemistry 1987; 262: 1420–1424
   PubMedGoogle Scholar
• Ito A., Ogishima T., Ou W., Omura T., Aoyagi H., Lee S., Mihara H., Izumiya N. Effects of synthetic model peptides resembling the extension peptides of mitochondrial enzyme precursors on import of the precursors into mitochondria. Journal of Biochemistry 1985; 98: 1571–1582
   Google Scholar
• Jacobs R. E., White S. H. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry 1989; 28: 3421–2437
   PubMed Web of Science ®Google Scholar
• Kumamoto T., Morohashi K., Ito A., Omura T. Site-directed mutagenesis of basic amino acid residues in the extension peptide of P-450 (SCC) precursor: effects on the import of the precursor into mitochondria. Journal of Biochemistry 1987; 102: 833–838
   Google Scholar
• Kumamoto T., Ito A., Omura T. Critical region in the extension peptide for the import of cytochrome P-450 (SCC) precursor into mitochondria. Journal of Biochemistry 1989; 105: 72–78
   Google Scholar
• Leenhouts J. M., De Gier J., De Kruijff B. A novel property of a mitochondrial presequence. Its ability to induce cardiolipin-specific interbilayer contacts which are dissociated by a transmembrane potential. FEBS Letters 1993; 327: 172–176
   Google Scholar
• Maduke M., Roise D. Import of a mitochondrial presequence into protein-free phospholipid vesicles. Science 1993; 260: 364–367
   Google Scholar
• Martin J., Mahlke K., Pfanner N. Role of an energized inner membrane in mitochondrial protein import. Δψ drives the movement of presequences. Journal of Biological Chemistry 1991; 266: 18051–18057
   PubMedGoogle Scholar
• Ou W.-J., Ito A., Umeda M., Inoue K., Omura T. Specific binding of mitochondrial protein precursors to liposomes containing cardiolipin. Journal of Biochemistry 1988; 103: 589–595
   Google Scholar
• Pfanner N., Weinzierl A. Minireview. Mechanisms of mitochondrial protein import. International Journal of Biochemistry 1992; 24: 65–69
   Google Scholar
• Roise D., Theiler F., Horvath S. J., Tomick J. M., Richards J. H., Allison D. S., Schatz G. Amphiphilicity is essential for mitochondrial presequence function. EMBO Journal 1988; 7: 649–653
   PubMedGoogle Scholar
• Rouser G., Fleischer S., Yamamoto A. Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 1970; 5: 494–496
   PubMed Web of Science ®Google Scholar
• Tamm L. K. Review. Membrane insertion and lateral mobility of synthetic amphiphilic signal peptides in lipid model membranes. Biochimica et Biophysica Acta 1991; 1071: 123–148
   Google Scholar
• Török Z., Demel R. A., Leenhouts J. M., De Kruijff B. Presequence mediated intermembrane contact formation and lipid flow. A model membrane study. Biochemistry 1994; 33: 5589–5594
   Google Scholar
• Von Heijne G. Mitochondrial targeting sequences may form amphiphilic helices. EMBO Journal 1986; 5: 1335–1342
   PubMed Web of Science ®Google Scholar
• Wang Y., Weiner H. The presequence of rat liver aldehyde dehydrogenase requires the presence of an α-helix at its N-terminal region, which is stabilized by the helix at its C-termini. Journal of Biological Chemistry 1993; 268: 4759–4765
   Google Scholar