Detection, isolation and some properties of membrane proteinases from yeast mitochondria.
Three cytochrome c hydrolase species were found in the 0.05% SDS extract from submitochondrial particles. Their polypeptides all have a molecular weight of 17 000 but differ in pI values (4.0, 4.2 and 4.4), as shown by SDS-polyacrylamide gel electrophoresis and polyacrylamide gel isoelectric focusing. The activity of pooled cytochrome c hydrolases is sensitive to PMSF, pCMPS , and leupeptin but insensitive to EDTA or o-phenanthroline. Besides the cytochrome c-hydrolyzing enzymes, the SDS extract contains three protein components with BAPA ( BANA )-hydrolyzing activity, which also show similar molecular weights (17 5000) but different pI values (4.2, 4.3 and 4.7). It is supposed that at least some of the enzymes mentioned are involved in the intramembrane proteolysis of polypeptides synthesized on mitoribosomes .
D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013367:Submitochondrial Particles / Q000201:enzymology; D013379:Substrate Specificity
D011480:Protease Inhibitors; D010450:Endopeptidases; D010447:Peptide Hydrolases; C039284:cytochrome C hydrolase