Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase.
Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase.
复制标题
全功能 F1Fo ATP 合酶中 c 亚基寡聚物的旋转。
DOI：
10.1073/pnas.98.3.898
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发表时间：
2001
影响因子：
11.1
通讯作者：
Capaldi,RA
中科院分区：
文献类型：
--
作者：
Tsunoda,SP;Aggeler,R;Yoshida,M;Capaldi,RA
F1FO型三磷酸腺苷合成酶是已知的最小的运动酶。以前的研究已经证实，在催化过程中，F1部分的中心γ和ɛ亚基相对于α3、β3和δ亚基的定子旋转。我们现在证明，FOPAT中的c亚基环与γ和ɛ亚基一起移动。这是通过在γ，ɛ和c亚基之间的界面上遗传引入的半胱氨酸残基之间的二硫键连接三个转子亚基来证明的。通过使用CuCl2诱导氧化，实现了γ，ɛ和c亚基的基本完全交联。这三个亚基的结合对ATP水解、质子转运或ATP合成没有显著影响，并且这些功能中的每一个都保持了抑制剂的敏感性。这些结果明确地将c亚基低聚物置于该分子机器的转子部分。
The F1Fo-type ATP synthase is the smallest motor enzyme known. Previous studies had established that the central γ and ɛ subunits of the F1part rotate relative to a stator of α3β3and δ subunits during catalysis. We now show that the ring of c subunits in the Fopart moves along with the γ and ɛ subunits. This was demonstrated by linking the three rotor subunits with disulfide bridges between cysteine residues introduced genetically at the interfaces between the γ, ɛ, and c subunits. Essentially complete cross-linking of the γ, ɛ, and c subunits was achieved by using CuCl2to 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.