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.
journal_name
Proc Natl Acad Sci U S Aauthors
Friedl P,Bienhaus G,Hoppe J,Schairer HUdoi
10.1073/pnas.78.11.6643subject
Has Abstractpub_date
1981-11-01 00:00:00pages
6643-6issue
11eissn
0027-8424issn
1091-6490journal_volume
78pub_type
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