AT(D)PMg-induced dissociation of the α3β3complex of the F1-ATPase from a thermophilicBacillusPS3 into α1β1heterodimers is prevented by mutation β(Y341C)

Abstract
AT(D)PMg induces dissociation of the α3β3 complex of F1‐ATPase from a thermophilic Bacillus strain, PS3, into the α1β1 heterodimers [(1991) Biochim. Biophys. Acta 1056, 279‐284] but the location of the AT(D)PMg binding site responsible is not known. From the analysis of AT(D)PMg binding properties of the isolated mutant β subunit, β(y341c) and the stability of the α3β(y341c)3 complex in the presence of AT(D)PMg, we conclude that binding of AT(D)PMg to the Tyr‐341 site of the β subunit(s) in the α3β3 complex triggers the dissociation of the α3β3 complex into the α1β1 heterodimers.

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