Mitochondrial ATPase complex of Aspergillus nidulans and the dicyclohexylcarbodiimide-binding protein.
The dicyclohexylcarbodiimide-binding protein of Aspergillus nidulans has been identified as the smallest subunit of the mitochondrial ATPase complex, and has a molecular weight of approximately 8000. It is extractable from whole mitochondria and from the purified enzyme in neutral chloroform/methanol, contains 30% polar amino acids, and the N-terminal amino acid has been identified as tyrosine. Using a double-labelling technique in the absence and presence of cycloheximide, followed by immunoprecipitation of the enzyme complex with antiserum against Neuospora crassa F1 ATPase, it has been shown that this subunit is synthesized on cytoplasmic ribosomes.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001233:Aspergillus nidulans / Q000201:enzymology*; D002234:Carbodiimides / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D003513:Cycloheximide / Q000494:pharmacology; D004024:Dicyclohexylcarbodiimide / Q000378:metabolism*; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D011233:Precipitin Tests
D000596:Amino Acids; D002234:Carbodiimides; D002352:Carrier Proteins; D046911:Macromolecular Substances; D004024:Dicyclohexylcarbodiimide; D003513:Cycloheximide; D000251:Adenosine Triphosphatases