Assembly of the mitochondrial system. Purification of a mitochondrial product of the ATPase.
A low-molecular-weight protein synthesized in yeast mitochondria was purified. The protein was identified as a component of the rutamycin-sensitive ATPase. The amino-acid composition of the purified protein shows an extremely large preponderance of nonpolar residues, which may account for its solubility in chloroform-methanol. Indirect evidence suggests that this component is involved in the conferral of rutamycin sensitivity and may also have a function in the assembly of the ATPase complex.
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000596:Amino Acids / Q000032:analysis; D000935:Antifungal Agents; D002250:Carbon Radioisotopes; D002855:Chromatography, Thin Layer; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000032:analysis / Q000096:biosynthesis / Q000302:isolation & purification*; D007118:Immunoassay; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism*; D008970:Molecular Weight; D011233:Precipitin Tests; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D014316:Tritium
D000596:Amino Acids; D000935:Antifungal Agents; D002250:Carbon Radioisotopes; D005656:Fungal Proteins; D014316:Tritium; D000251:Adenosine Triphosphatases