AT(D)PMg-induced dissociation of the alpha 3 beta 3 complex of the F1-ATPase from a thermophilic Bacillus PS3 into alpha 1 beta 1 heterodimers is prevented by mutation beta (Y341C).
AT(D)PMg induces dissociation of the alpha 3 beta 3 complex of F1-ATPase from a thermophilic Bacillus strain. PS3, into the alpha 1 beta 1 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 beta subunit, beta(Y341C), and the stability of the alpha 3 beta(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 beta subunit(s) in the alpha 3 beta 3 complex triggers the dissociation of the alpha 3 beta 3 complex into the alpha 1 beta 1 heterodimers.
Kaibara
C
C
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Odaka
M
M
Hisabori
T
T
Yoshida
M
M
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D001407:Bacillus / Q000201:enzymology*; D002942:Circular Dichroism; D046911:Macromolecular Substances; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014443:Tyrosine / Q000737:chemistry
D046911:Macromolecular Substances; D014443:Tyrosine; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases