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β（Y341C）突变可阻止AT（D）PMg诱导嗜热芽孢杆菌PS3的F1-ATP酶的α3β3复合物解离成α1β1异二聚体。

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).

作者信息

Kaibara C, Odaka M, Hisabori T, Yoshida M

机构信息

Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.

出版信息

FEBS Lett. 1993 Apr 19;321(1):46-50. doi: 10.1016/0014-5793(93)80618-5.

DOI:10.1016/0014-5793(93)80618-5
PMID:8467909
Abstract

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.

摘要

AT(D)PMg可诱导嗜热芽孢杆菌菌株PS3的F1-ATP酶的α3β3复合物解离成α1β1异二聚体[(1991)生物化学与生物物理学报1056, 279 - 284]，但负责此作用的AT(D)PMg结合位点的位置尚不清楚。通过对分离出的突变体β亚基β(Y341C)的AT(D)PMg结合特性以及在AT(D)PMg存在下α3β(Y341C)3复合物稳定性的分析，我们得出结论：AT(D)PMg与α3β3复合物中β亚基的Tyr - 341位点结合会触发α3β3复合物解离成α1β1异二聚体。

相似文献

1
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).β（Y341C）突变可阻止AT（D）PMg诱导嗜热芽孢杆菌PS3的F1-ATP酶的α3β3复合物解离成α1β1异二聚体。
FEBS Lett. 1993 Apr 19;321(1):46-50. doi: 10.1016/0014-5793(93)80618-5.
2
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In vivo affinity label of a protein expressed in Escherichia coli. Coenzyme A occupied the AT(D)P binding site of the mutant F1-ATPase beta subunit (Y307C) through a disulfide bond.大肠杆菌中表达的蛋白质的体内亲和标记。辅酶A通过二硫键占据了突变型F1-ATP酶β亚基（Y307C）的AT（D）P结合位点。
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Tyr-341 of the beta subunit is a major Km-determining residue of TF1-ATPase: parallel effect of its mutations on Kd(ATP) of the beta subunit and on Km(ATP) of the alpha 3 beta 3 gamma complex.
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