title: The regulatory C-terminal domain of subunit ε of F₀F₁ ATP synthase is dispensable for growth and survival of Escherichia coli.
abstract: The C-terminal domain of subunit ε of the bacterial F₀F₁ ATP synthase is reported to be an intrinsic inhibitor of ATP synthesis/hydrolysis activity in vitro, preventing wasteful hydrolysis of ATP under low-energy conditions. Mutants defective in this regulatory domain exhibited no significant difference in growth rate, molar growth yield, membrane potential, or intracellular ATP concentration under a wide range of growth conditions and stressors compared to wild-type cells, suggesting this inhibitory domain is dispensable for growth and survival of Escherichia coli.
authors.affiliation: Department of Microbiology and Immunology, Otago School of Medical Sciences, University of Otago, Dunedin, New Zealand.
authors.forename: Naohiro
authors.initials: N
authors.lastname: Taniguchi
authors.forename: Toshiharu
authors.initials: T
authors.lastname: Suzuki
authors.forename: Michael
authors.initials: M
authors.lastname: Berney
authors.forename: Masasuke
authors.initials: M
authors.lastname: Yoshida
authors.forename: Gregory M
authors.initials: GM
authors.lastname: Cook
mesh_terms: D004926:Escherichia coli / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics* / Q000378:metabolism*; D050296:Microbial Viability; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism*; D017384:Sequence Deletion
chemical_list: D029968:Escherichia coli Proteins; C496259:F0F1-ATPase epsilon subunit, E coli; D006180:Proton-Translocating ATPases