The dicyclohexylcarbodiimide-binding protein c of ATP synthase from Escherichia coli is not sufficient to express an efficient H+ conduction.
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.
D025181:ATP Synthetase Complexes; D000244:Adenosine Diphosphate / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D001693:Biological Transport, Active / Q000187:drug effects; D002352:Carrier Proteins / Q000378:metabolism*; D003488:Cyanogen Bromide; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000302:isolation & purification; D009097:Multienzyme Complexes / Q000378:metabolism*; D009154:Mutation; D010446:Peptide Fragments / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*
D000596:Amino Acids; D002352:Carrier Proteins; D008565:Membrane Proteins; D009097:Multienzyme Complexes; D010446:Peptide Fragments; D004024:Dicyclohexylcarbodiimide; D000244:Adenosine Diphosphate; D010770:Phosphotransferases; D025181:ATP Synthetase Complexes; D003488:Cyanogen Bromide