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  • Title: A mutation in the alpha-subunit of F1-ATPase from Escherichia coli affects the binding of F1 to the membrane.
    Author: Maggio MB, Parsonage D, Senior AE.
    Journal: J Biol Chem; 1988 Apr 05; 263(10):4619-23. PubMed ID: 2895104.
    Abstract:
    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.
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