title: Studies on essential amino acid residues and functional regions of H+-ATPase (F0F1) from Escherichia coli by gene manipulation.
abstract: 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.
authors.affiliation: Department of Organic Chemistry and Biochemistry, Institute of Scientific and Industrial Research, Osaka, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Noumi
authors.forename: M
authors.initials: M
authors.lastname: Takeyama
authors.forename: M
authors.initials: M
authors.lastname: Kuki
authors.forename: M
authors.initials: M
authors.lastname: Maeda
authors.forename: M
authors.initials: M
authors.lastname: Futai
mesh_terms: 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
chemical_list: D006180:Proton-Translocating ATPases