Studies on essential amino acid residues and functional regions of H+-ATPase (F0F1) from Escherichia coli by gene manipulation.
We discussed application of in vitro mutagenesis on H+-ATPase (F0F1) of Escherichia coli. The oligonucleotide-directed site specific mutagenesis and construction of a set of truncated subunits were useful for identifying essential residues of beta subunit and a functional region of epsilon subunit, respectively, of this complicated membrane enzyme.
Noumi
T
T
Department of Organic Chemistry and Biochemistry, Institute of Scientific and Industrial Research, Osaka, Japan.
Takeyama
M
M
Kuki
M
M
Maeda
M
M
Futai
M
M
D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D005818:Genetic Engineering / Q000379:methods; D008969:Molecular Sequence Data; D009154:Mutation; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism
D006180:Proton-Translocating ATPases