Mitochondrial ATPase Complex of Aspergillus nidulans and the Dicyclohexylcarbodiimide‐Binding Protein

Abstract

The dicyclohexylcarbodiimide-binding protein of A. nidulans was identified as the smallest subunit of the mitochondrial ATPase complex and has a MW of .apprx. 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 was identified as tyrosine. Using a double-labeling technique in the absence and presence of cycloheximide, followed by immunoprecipitation of the enzyme complex with antiserum against N. crassa F1 ATPase, it was shown that this subunit is synthesized on cytoplasmic ribosomes.