期刊论文详细信息
FEBS Letters
AT(D)PMg‐induced dissociation of the α3β3 complex of the F1‐ATPase from a thermophilic Bacillus PS3 into α1β1 heterodimers is prevented by mutation β(Y341C)
Hisabori, Toru1  Kaibara, Chitose2  Odaka, Masafumi3  Yoshida, Masasuke2 
[1] Department of Biology, Yokohama City University, Seto, Yokohama 236, Japan;Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 227, Japan;The Tokyo Metropolitan Institute of Medical Science, Honkomagome, Tokyo 113, Japan
关键词: F1-ATPase;    α3β3 complex of F1;    α1β1 heterodimer of F1;    ATP-induced dissociation;    CD;    circular dichroism;    HPLC;    high performance liquid chromatography;    TF1;    and EF1;    F1-ATPases from a thermophilic Bacillus strain PS3;    and E. coli;    respectively;   
DOI  :  10.1016/0014-5793(93)80618-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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.

【 授权许可】

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