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首页> 美国卫生研究院文献>PLoS Clinical Trials >The Torque of Rotary F-ATPase Can Unfold Subunit Gamma If Rotor and Stator Are Cross-Linked
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The Torque of Rotary F-ATPase Can Unfold Subunit Gamma If Rotor and Stator Are Cross-Linked

机译：如果转子和定子交联，则旋转F-ATPase的扭矩可以展开亚基γ

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摘要

During ATP hydrolysis by F1-ATPase subunit γ rotates in a hydrophobic bearing, formed by the N-terminal ends of the stator subunits (αβ)3. If the penultimate residue at the α-helical C-terminal end of subunit γ is artificially cross-linked (via an engineered disulfide bridge) with the bearing, the rotary function of F1 persists. This observation has been tentatively interpreted by the unfolding of the α-helix and swiveling rotation in some dihedral angles between lower residues. Here, we screened the domain between rotor and bearing where an artificial disulfide bridge did not impair the rotary ATPase activity. We newly engineered three mutants with double cysteines farther away from the C-terminus of subunit γ, while the results of three further mutants were published before. We found ATPase and rotary activity for mutants with cross-links in the single α-helical, C-terminal portion of subunit γ (from γ285 to γ276 in E. coli), and virtually no activity when the cross-link was placed farther down, where the C-terminal α-helix meets its N-terminal counterpart to form a supposedly stable coiled coil. In conclusion, only the C-terminal singular α-helix is prone to unwinding and can form a swivel joint, whereas the coiled coil portion seems to resist the enzyme's torque.
机译：在F1-ATPase水解ATP的过程中，γ会在疏水轴承中旋转，该轴承由定子亚基（αβ）3的N端形成。如果亚基γ的α-螺旋C末端的倒数第二个残基通过轴承人工交联（通过工程化的二硫键），则F1的旋转功能仍然存在。该观察已通过α-螺旋的展开和较低残基之间的某些二面角的旋转旋转进行了初步解释。在这里，我们筛选了转子和轴承之间的区域，在该区域中，人工二硫键不会损害旋转ATPase的活性。我们新设计了三个双半胱氨酸突变体，它们距离γ亚基的C末端较远，而另外三个突变体的结果已在之前发表。我们发现γ亚基的单个α螺旋，C端部分（在大肠杆菌中从γ285到γ276）具有交联的突变体具有ATPase和旋转活性，而当交联越靠下时，则几乎没有活性。 ，其中C末端的α螺旋与N末端的螺旋相遇，从而形成了一个稳定的盘绕线圈。总之，只有C末端的奇异α螺旋易于解旋并可以形成旋转接头，而盘绕的螺旋部分似乎抵抗了酶的扭矩。

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