title: Mutagenic analysis of the F0 stator subunits.
abstract: The a and b subunits constitute the stator elements in the F0 sector of F1F0-ATP synthase. Both subunits have been difficult to study by physical means, so most of the information on structure and function relationships in the a and b subunits has been obtained using mutagenesis in combination with biochemical methods. These approaches were used to demonstrate that the a subunit in association with the ring of c subunits houses the proton channel through F1F0-ATP synthase. The map of the amino acids contributing to the proton channel is probably complete. The two b subunits dimerize, forming an extended flexible unit in the peripheral stalk linking the F1 and F0 sectors. The unique characteristics of specific amino acid substitutions affecting the a and b subunits suggested differential effects on rotation during F1F0-ATPase activity.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of Florida, Gainesville 32610, USA. bcain@biochem.med.ufl.edu
authors.forename: B D
authors.initials: BD
authors.lastname: Cain
mesh_terms: D001419:Bacteria / Q000201:enzymology; D006801:Humans; D016296:Mutagenesis; D009154:Mutation; D021122:Protein Subunits; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D021122:Protein Subunits; D011994:Recombinant Proteins; D006180:Proton-Translocating ATPases