A mutation in the alpha-subunit of F1-ATPase from Escherichia coli affects the binding of F1 to the membrane.
The mutation Gly-29----Asp in the alpha-subunit of the F1-ATPase from Escherichia coli was characterized and shown to cause the following effects. 1) Oxidative phosphorylation was markedly impaired in vivo 2) Membrane ATPase and ATP-driven proton-pumping activities were decreased markedly. 3) Membranes were proton-permeable, and membrane-bound ATPase was dicyclohexylcarbodiimide-insensitive. Therefore, it appeared that integration between F1 and F0 was abnormal. This was confirmed directly by the demonstration that the mutant F1 bound poorly to stripped membranes from a normal strain. Purified, soluble mutant F1 had normal ATPase activity. These results suggest that residue Gly-29, which is strongly conserved in alpha-subunits of F1-ATPases, lies in a region of the alpha-subunit important for membrane binding. Thus, three regions of the F1-alpha-subunit have now been recognized, specialized for membrane binding, nucleotide binding, and alpha/beta intersubunit signal transmission, respectively. The approximate locations of the three regions are described.
D000483:Alleles; D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000201:enzymology; D004277:DNA, Single-Stranded / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009154:Mutation; D010957:Plasmids; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism; D013045:Species Specificity
D004277:DNA, Single-Stranded; D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases