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. 1992 Jul;174(13):4496–4499. doi: 10.1128/jb.174.13.4496-4499.1992

Mutational analysis of the glycine-rich region of the c subunit of the Escherichia coli F0F1 ATPase.

U Norris 1, P E Karp 1, A L Fimmel 1
PMCID: PMC206237  PMID: 1385593

Abstract

Eight strains carrying amino acid substitutions within the c subunit of the F0F1 ATPase of Escherichia coli have been constructed by using site-directed mutagenesis. Three strains carrying the substitutions Gly-23----Leu, Ala-24----Leu, and Gly-38----Leu, which reside in or near the highly conserved glycine-rich region of the c subunit, are unable to carry out oxidative phosphorylation. Membranes prepared from these strains possess basal levels of ATPase activity. In contrast, strains carrying the substitutions Ile-30----Phe, Gly-33----Leu, Gly-58----Leu, and Lys-34----Val and the Lys-34----Val, Glu-37----Gln double substitution were found to possess a coupled phenotype similar to that of the wild type.

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Selected References

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