Proteolysis of the products of mitochondrial protein synthesis in yeast mitochondria and submitochondrial particles.
Degradation of mitochondrial translation products in Saccharomyces cerevisiae mitochondria was studied by selectively labelling these entities in vivo in the presence of cycloheximide and following their fate in isolated mitochondria. One-third to one-half of the mitochondrial translation products are shown to be degraded, depending on the culture growth phase, with an approximate half-life of 35 min. This process is shown to be ATP-dependent, enhanced in the presence of puromycin and inhibited by chloramphenicol. Further, the proteolysis is suppressed by detergents and is insensitive to antisera against yeast proteinases A and B when measured in mitochondria or 'inside-out' submitochondrial particles. It is concluded that the breakdown of mitochondrial translation products is most probably due to the action of endogenous proteinase(s) associated with the mitochondrial inner membrane. This proteinase is inhibited by phenylmethanesulphonyl fluoride, leupeptin, antipain and chymostatin.
D000255:Adenosine Triphosphate / Q000378:metabolism; D002701:Chloramphenicol / Q000494:pharmacology; D008928:Mitochondria / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D010940:Plant Proteins / Q000096:biosynthesis*; D011480:Protease Inhibitors / Q000494:pharmacology; D014176:Protein Biosynthesis; D011691:Puromycin / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000201:enzymology / Q000378:metabolism
D010940:Plant Proteins; D011480:Protease Inhibitors; D011691:Puromycin; D002701:Chloramphenicol; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases