Effects of Synthetic Model Peptides Resembling the Extension Peptides of Mitochondrial Enzyme Precursors on Import of the Precursors into Mitochondria1
- 1 December 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 98 (6), 1571-1582
- https://doi.org/10.1093/oxfordjournals.jbchem.a135426
Abstract
One common and characteristic feature of the extension peptides of mitochondrial enzyme precursors is the presence of repeating short stretches of uncharged amino acids linked by basic amino acids. We synthesized several model peptides having this particular feature of the extension peptides. The peptides contained arginine or lysine as a basic amino acid residue linking sequences of two to four residues of leucine and alanine. We examined the effects of the peptides on the import of the precursors of two mitochondrial enzymes, cytochrome P-450(SCC) and adrenodoxin, and found that the peptides were generally inhibitory to the import of the precursors into mitochondria. The effective concentrations of some of the inhibitory peptides were as low as a few μM. The peptides containing lysine instead of arginine had an essentially similar inhibitory effect on the import. The peptides did not inhibit the binding of pre-P450(SCC) to the surface of mitochondria. The synthetic model peptides uncoupled oxidative phosphorylation of mitochondria prepared from either rat liver or bovine adrenal cortex, and induced leakage of enzymes from the inner compartments of mitochondria. However, the synthetic model peptides did not solubilize membrane-bound enzymes from mitochondria, suggesting that their effect on the membranes is different from that of detergents. The synthetic model peptides seem to bind to the membranes causing significant perturbation in the membrane structure, which is possibly related to the functions of the particular common sequence found in the extension peptides of mitochondrial enzyme precursors.Keywords
This publication has 17 references indexed in Scilit:
- Transport of the Precursor for Sulfite Oxidase into Intermembrane Space of Liver Mitochondria: Characterization of Import and Processing Activities1The Journal of Biochemistry, 1984
- Import of proteins into mitochondria: nucleotide sequence of the gene for a 70-kd protein of the yeast mitochondrial outer membrane.The EMBO Journal, 1983
- Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the F1-ATPase beta subunit.Journal of Biological Chemistry, 1983
- Molecular cloning and sequence determination of the nuclear gene coding for mitochondrial elongation factor Tu of Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences, 1983
- Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre sequence for protein transport into mitochondria.Journal of Biological Chemistry, 1982
- The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA.The EMBO Journal, 1982
- β-turns in proteinsJournal of Molecular Biology, 1977
- Turnover of Constituents of the Endoplasmic Reticulum Membranes of Rat HepatocytesJournal of Biological Chemistry, 1967
- Techniques for the application of polarography to mitochondrial respirationBiochimica et Biophysica Acta, 1961
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951