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).
Fimmel
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Department of Biochemistry, Faculty of Science, Australian National University, Canberra.
Norris
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D002462:Cell Membrane / Q000201:enzymology; D004262:DNA Restriction Enzymes; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D005453:Fluorescence; D005998:Glycine; D009154:Mutation; D009243:NAD / Q000494:pharmacology; D010957:Plasmids; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D011796:Quinacrine; D013329:Structure-Activity Relationship; D014169:Transformation, Bacterial; D014633:Valine
D009243:NAD; D004262:DNA Restriction Enzymes; D006180:Proton-Translocating ATPases; D011796:Quinacrine; D014633:Valine; D005998:Glycine