Biogenesis of the mitochondrial ATPase from sea urchin embryos.
The mitochondrial rutamycin-sensitive ATPase from sea urchin eggs was purified to homogeneity. The subunit structure of the enzyme was characterized by SDS-gel electrophoresis. Eight polypeptides were identified with molecular weights of 55,000, 52,000, 39,000, 31,000, 28,000, 23,000, 17,000 and 10,000. Developing sea urchin embryos were incubated with [2H]leucine in the presence of emetine preferentially to label mitochondrially made proteins. Under these conditions sea urchin mitochondria synthesize eight different polypeptides. Two of these proteins, with molecular weights of 31,000 and 23,000, co-purify with the ATPase. Antibody directed against the pure rutamycin-sensitive ATPase precipitated only these two proteins. Therefore, two of the eight sea urchin ATPase subunits appear to be made by mitochondria.
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000096:biosynthesis* / Q000302:isolation & purification; D000818:Animals; D007163:Immunosorbent Techniques; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D010455:Peptides / Q000302:isolation & purification; D012427:Rutamycin / Q000494:pharmacology; D012617:Sea Urchins / Q000196:embryology* / Q000201:enzymology
D010455:Peptides; D012427:Rutamycin; D000251:Adenosine Triphosphatases