title: Identification of a mutation in Escherichia coli F1-ATPase beta-subunit conferring resistance to aurovertin.
abstract: A mutation conferring aurovertin resistance on Escherichia coli F1-ATPase was identified as R398----H in the F1 beta-subunit. Beta-subunit from the mutant does not bind aurovertin; therefore our results suggest the region of sequence around residue beta-398 is involved in aurovertin binding. Since nucleotide and aurovertin binding to isolated beta-subunit are not mutually exclusive, the data further suggest that the beta-subunit catalytic nucleotide-binding domain does not include residue 398. The mutation prevented aurovertin inhibition of ATPase at pH 6 and 8.5, implying charge on the arginine side-chain is not a major determinant of aurovertin binding or that the pK of R398 is shifted due to a peculiar environment. The equivalent residue is usually arginine in F1 beta-subunits of different species; notably in the aurovertin-insensitive thermophilic bacterium PS3 F1-ATPase, this residue is phenylalanine.
authors.affiliation: Department of Biochemistry, University of Rochester Medical Center, NY 14642.
authors.forename: R S
authors.initials: RS
authors.lastname: Lee
authors.forename: J
authors.initials: J
authors.lastname: Pagan
authors.forename: M
authors.initials: M
authors.lastname: Satre
authors.forename: P V
authors.initials: PV
authors.lastname: Vignais
authors.forename: A E
authors.initials: AE
authors.lastname: Senior
mesh_terms: D001313:Aurovertins / Q000494:pharmacology*; D001665:Binding Sites; D003001:Cloning, Molecular; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000235:genetics*; D011714:Pyrans / Q000494:pharmacology*
chemical_list: D001313:Aurovertins; D011714:Pyrans; D006180:Proton-Translocating ATPases