Mutational analysis of the glycine-rich region of the c subunit of the Escherichia coli F0F1 ATPase.
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.
Norris
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Division of Biochemistry and Molecular Biology, School of Life Science, Faculty of Science, Australian National University, Canberra, A.C.T.
Karp
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Fimmel
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D004269:DNA, Bacterial / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005838:Genotype; D005998:Glycine; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides; D010957:Plasmids; D006180:Proton-Translocating ATPases / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity
D004269:DNA, Bacterial; D046911:Macromolecular Substances; D009838:Oligodeoxyribonucleotides; D006180:Proton-Translocating ATPases; D005998:Glycine