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首页> 外文期刊>Biochemistry >Unique structural modulation of a non-native substrate by cochaperone DnaJ
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Unique structural modulation of a non-native substrate by cochaperone DnaJ

机译：伴侣蛋白DnaJ对非天然底物的独特结构调节

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The role of bacterial DnaJ protein as a cochaperone of DnaK is strongly appreciated. Although DnaJ unaccompanied by DnaK can bind unfolded as well as native substrate proteins, its role as an individual chaperone remains elusive. In this study, we demonstrate that DnaJ binds a model non-native substrate with a low nanomolar dissociation constant and, more importantly, modulates the structure of its non-native state. The structural modulation achieved by DnaJ is different compared to that achieved by the DnaK-DnaJ complex. The nature of structural modulation exerted by DnaJ is suggestive of a unique unfolding activity on the non-native substrate by the chaperone. Furthermore, we demonstrate that the zinc binding motif along with the C-terminal substrate binding domain of DnaJ is necessary and sufficient for binding and the subsequent binding-induced structural alterations of the non-native substrate. We hypothesize that this hitherto unknown structural alteration of non-native states by DnaJ might be important for its chaperoning activity by removing kinetic traps of the folding intermediates.
机译：细菌DnaJ蛋白作为DnaK的伴侣蛋白的作用受到高度赞赏。尽管不伴随DnaK的DnaJ可以结合展开的以及天然底物蛋白，但其作为单个分子伴侣的作用仍然难以捉摸。在这项研究中，我们证明DnaJ结合具有低纳摩尔解离常数的模型非天然底物，更重要的是，调节其非天然状态的结构。 DnaJ实现的结构调制与DnaK-DnaJ复合体实现的结构调制不同。 DnaJ施加的结构调节的性质表明，伴侣分子在非天然底物上具有独特的展开活性。此外，我们证明锌结合基序以及DnaJ的C端底物结合结构域对于结合和随后的结合诱导的非天然底物的结构改变是必要和充分的。我们假设，DnaJ迄今未知的非自然状态的结构改变，可能对它的伴侣活动很重要，因为它可以消除折叠中间体的动力学陷阱。

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