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PubMed1989

The F1F0-ATPase of Escherichia coli. The substitution of glycine by valine at position 29 in the c-subunit affects function but not assembly.

Site-directed mutagenesis has been used to construct two mutations within the uncE gene, coding for the c-subunit of the F1F0-ATPase, resulting in the substitution of Gly-29 by Val and Gly-18 by Leu. The strain carrying the Gly-29----Val substitution is unable to grow on succinate as sole carbon source and possesses an uncoupled growth yield, while the strain carrying the Gly-18----Leu substitution possesses a wild-type phenotype. Membranes prepared from the strain carrying the Gly-29----Val substitution possess low levels of ATPase activity and are proton-impermeable. The F1-ATPase activity of this strain was found to be inhibited by approx. 75% when bound to the membrane. These results are discussed in relation to a previously proposed model for the F0 (Cox, G.B., Fimmel, A.L., Gibson, F. and Hatch, L. (1986) Biochim. Biophys. Acta 849, 62-69).

Cell Membrane↗