Abstract
The N,N'-dicyclohexylcarbodiimide-binding proteolipid subunit of the mitochondrial adenosinetriphosphatases (ATP phosphohydrolase, EC 3.6.1.3) of Neurospora crassa and Saccharomyces cerevisiae were purified from mitochondria incubated with the radioactively labeled inhibitor. The specifically labeled subunit was cleaved with cyanogen bromide and N-bromosuccinimide, and the resultant fragments were separated by gel chromatography in the presence of 80% (vol/vol) formic acid. The N,N'-dicyclohexylcarbodiimide label was recovered in each organism exclusively in a 17-residue fragment. Further analysis by automated solid-phase Edman degradation revealed that the bound label was present at only one position, corresponding to a glutamyl residue. The N,N'-dicyclohexylcarbodiimide-modified glutamyl residue is the only identical acidic position in both proteins and occurs in the middle of a hydrophobic sequence of about 25 residues.
MeSH Terms
Adenosine Triphosphatases/antagonists & inhibitors
Amino Acid Sequence
Binding Sites
Carbodiimides/pharmacology
Dicyclohexylcarbodiimide/metabolism,pharmacology
Glutamates/metabolism
Mitochondria/enzymology
Neurospora crassa/enzymology
Peptide Fragments
Proteolipids/metabolism
Saccharomyces cerevisiae/enzymology
Chemicals
Carbodiimides
Glutamates
Peptide Fragments
Proteolipids
Dicyclohexylcarbodiimide
Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sebald W
Machleidt W
Wachter E
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25 references, click to expand
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