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The Dicyclohexylcarbodiimide-Binding Protein c of ATP Synthase from Escherichia coli is not Sufficient to Express an Efficient H+ Conduction
Peter Friedl, Gerhard Bienhaus, Jurgen Hoppe and Hans Ulrich Schairer
Proceedings of the National Academy of Sciences of the United States of America
Vol. 78, No. 11, [Part 2: Biological Sciences] (Nov., 1981), pp. 6643-6646
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/11319
Page Count: 4
You can always find the topics here!Topics: Fluorescence, Amino acids, Biochemistry, Bacteriophage mu, Chemical suspensions, Adenosine triphosphatases, Congenic strains, Acridines, Dyes, Escherichia coli
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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.
Proceedings of the National Academy of Sciences of the United States of America © 1981 National Academy of Sciences