Identification of a mutation in Escherichia coli F1‐ATPase β‐subunit conferring resistance to aurovertin
- 14 August 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 253 (1-2), 269-272
- https://doi.org/10.1016/0014-5793(89)80973-1
Abstract
A mutation conferring aurovertin resistance on Escherichia coli F1-ATPase was identified as R398 → in the F1 β-subunit. β-subunit from the mutant doe not bind aurovertin; therefore our results suggest the region of sequence around residue β-398 is involved in aurovertin binding. Since nucleotide and aurovertin binding to isolated β-subunit are not mutually exclusive, the data further suggest that the β-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 β-subunits of different species; notably in the aurovertin-insensitive thermophilic bacterium PS3 F1-ATPase, this residue is phenylalanine.Keywords
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