Open AccessMitochondrial ATPase Complex of Aspergillus nidulans and the Dicyclohexylcarbodiimide‐Binding Protein
Author(s) -
TURNER Geoffrey,
IMAM Gamal,
KÜNTZEL Hans
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb13145.x
Subject(s) - neurospora crassa , protein subunit , biochemistry , aspergillus nidulans , atpase , cycloheximide , biology , amino acid , immunoprecipitation , tyrosine , mitochondrion , enzyme , chemistry , microbiology and biotechnology , protein biosynthesis , gene , mutant
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 Neurospora crassa F 1 ATPase, it has been shown that this subunit is synthesized on cytoplasmic ribosomes.