Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

被引:123
作者
Tsunoda, SP
Aggeler, R
Yoshida, M
Capaldi, RA [1 ]
机构
[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
[2] Tokyo Inst Technol, Res Lab Resources Utilizat, Yokohama, Kanagawa 2268503, Japan
[3] Teikyo Univ, Biotechnol Res Ctr 3F, Core Res Evolut Sci & Technol Genet Programming, Kawasaki, Kanagawa 2160001, Japan
关键词
D O I
10.1073/pnas.031564198
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The F1F0-type ATP synthase is the smallest motor enzyme known. Previous studies had established that the central gamma and epsilon subunits of the F-1 part rotate relative to a stator of alpha (3)beta (3) and delta subunits during catalysis. We now show that the ring of c subunits in the F-0 part moves along with the gamma and epsilon subunits. This was demonstrated by linking the three rotor subunits with disulfide bridges between cysteine residues introduced genetically at the interfaces between the gamma, epsilon, and c subunits. Essentially complete cross-linking of the gamma, epsilon, and c subunits was achieved by using CuCl2 to induce oxidation. This fixing of the three subunits together had no significant effect on ATP hydrolysis, proton translocation, or ATP synthesis, and each of these functions retained inhibitor sensitivity. These results unequivocally place the c subunit oligomer in the rotor part of this molecular machine.
引用
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页码:898 / 902
页数:5
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