The Dicyclohexylcarbodiimide-Binding Protein c of ATP Synthase from Escherichia coli is not Sufficient to Express an Efficient H+ Conduction
Abstract
Bacteriophage Mu was inserted into the unc genes of Escherichia coli. The resulting mutation AS12 had a polar effect on the unc operon: membranes of the mutant AS12 contained the dicyclohexylcarbodiimide-binding protein c and the protein a as sole subunits of the ATP synthase. It was shown by peptide mapping and amino acid analysis of the fragments that protein c from mutant AS12 was identical with the wild-type protein c. The absence of subunit b in mutant AS12 drastically lowered the H+ conduction dependent on the membrane-integrated moiety (F0) of the ATP synthase. This suggests that both subunits b and c are necessary for an efficient expression of H+ conduction.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- November 1981
- DOI:
- 10.1073/pnas.78.11.6643
- Bibcode:
- 1981PNAS...78.6643F