PMID:158358
| Citation |
Senior, AE, Fayle, DR, Downie, JA, Gibson, F and Cox, GB (1979) Properties of membranes from mutant strains of Escherichia coli in which the beta-subunit of the adenosine triphosphatase is abnormal. Biochem. J. 180:111-8 |
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| Abstract |
Five uncoupled mutant strains of Escherichia coli carrying mutations in the uncD gene have been studied. In each of these mutant strains the beta-subunit of the F1 portion of the membrane-bound adenosine triphosphatase is abnormal. In one of the mutant strains (carrying the uncD12 allele) in F1-ATPase aggregate was formed which was purified and found to have low ATPase activity. ATPase activity was absent in the other four strains and the abnormal beta-subunits were tightly bound to the membranes. However, membranes from these strains exhibited various proton permeabilities as indicated by NADH-dependent atebrin-fluorescence quenching and bound different amounts of normal F1-ATPase. The amounts of reconstitution of energy-linked reactions after the addition of normal F1-ATPase also varied depending on the mutant allele. It is apparent that considerable phenotypic variations can occur between strains carrying mutations in the same unc gene. |
| Links | |
| Keywords |
Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Alleles; Cell Membrane/enzymology; Chemical Phenomena; Chemistry; Electrophoresis; Escherichia coli/enzymology; Escherichia coli/genetics; Mutation; Protein Binding |
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