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首页> 外文期刊>Nucleic Acids Research >Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif
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Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif

机译：钒酸盐抑制细菌MutS的ATPase活性和DNA结合能力。 Walker A图案上的钒酸盐-MutS相互作用的结构模型

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摘要

MutS, a member of the ABC ATPases superfeamily, is a mismatch DNA-binding protein constituent of the DNA post-replicative mismatch repair system (MMRS). In this work, it is shown that the ATPase activity of Pseudomonas aeruginosa and Escherichia coli MutS is inhibited by ortho- and decavanadate. Structural comparison of the region involved in the ATP binding of E.coli MutS with the corresponding region of other ABC ATPases inhibited by vanadate, including the myosin-orthovanadate-Mg complex, showed that they are highly similar. From these results it is proposed that the orthovanadate inhibition of MutS ATPase can take place by a similar mechanism to that described for other ATPases. Docking of decavanadate on the ATP-binding region of MutS showed that the energetically more favorable interaction of this compound would take place with the complex MutS-ADP-Mg, suggesting that the inhibitory effect could be produced by a steric impediment of the protein ATP/ADP exchange. Besides the effect observed on the ATPase activity, vanadate also affects the DNA-binding capability of the protein, and partially inhibits the oligomerization of MurtS and the temperature-induced inactivation of the protein. From the results obtained, and considering that vanadate is an intracellular trace component, this compound could be considered as a new modulator of the MMRS.
机译：MutS是ABC ATPases超家族的成员，是DNA复制后错配修复系统（MMRS）的错配DNA结合蛋白成分。在这项工作中，表明铜绿假单胞菌和大肠杆菌MutS的ATPase活性被原癸酸和十癸酸盐抑制。大肠杆菌MutS的ATP结合区域与其他受钒酸盐抑制的ABC ATP酶的相应区域（包括肌球蛋白-原钒酸盐-镁复合物）的结构比较表明，它们高度相似。从这些结果表明，可以通过与针对其他ATP酶所描述的机制相似的机制来发生原钒酸盐对MutS ATPase的抑制。十钒酸盐在MutS的ATP结合区域上的对接表明，该化合物与复合物MutS-ADP-Mg的相互作用在能量上更有利，这表明该抑制作用可能是由于ATP / ADP交换。钒酸盐除了对ATPase活性有影响外，还影响蛋白质的DNA结合能力，并部分抑制MurtS的寡聚和温度诱导的蛋白质失活。根据获得的结果，并考虑到钒酸盐是细胞内微量成分，该化合物可被视为MMRS的新调节剂。

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