大肠杆菌DnaK中的一个革兰氏阴性特征片段对于与共伴侣蛋白DnaJ和GrpE的ATP依赖性协同功能至关重要。
A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE.
作者信息
Sugimoto Shinya, Higashi Chihana, Saruwatari Kozue, Nakayama Jiro, Sonomoto Kenji
机构信息
Laboratory of Microbial Technology, Division of Microbial Science and Technology, Department of Bioscience and Biotechnology, Faculty of Agriculture, Graduate School, Kyushu University, Hakozaki, Fukuoka, Japan.
出版信息
FEBS Lett. 2007 Jun 26;581(16):2993-9. doi: 10.1016/j.febslet.2007.05.055. Epub 2007 May 29.
We describe importance of the characteristic segment in ATPase domain of DnaK chaperone which is present in all gram-negative bacteria but is absent in all gram-positive bacteria. In vitro studies, ATPase activity, luciferase-refolding activity, and surface plasmon resonance analyses, demonstrated that a segment-deletion mutant DnaKDelta74-96 became defective in the cooperation with the co-chaperones DnaJ and GrpE. In addition, in vivo complementation assay showed that expression of DnaKDelta74-96 could not rescue the viability of Escherichia coli DeltadnaK mutant at 43 degrees C. Consequently, we suggest evolutionary significance for this DnaK ATPase domain segment in gram-negative bacteria towards the DnaK chaperone system.
我们描述了DnaK伴侣蛋白ATP酶结构域中特征性片段的重要性，该片段存在于所有革兰氏阴性菌中，而在所有革兰氏阳性菌中均不存在。体外研究、ATP酶活性、荧光素酶复性活性及表面等离子体共振分析表明，片段缺失突变体DnaKDelta74-96在与共伴侣蛋白DnaJ和GrpE的协作中出现缺陷。此外，体内互补试验表明，DnaKDelta74-96的表达无法挽救大肠杆菌DeltadnaK突变体在43℃时的生存能力。因此，我们认为革兰氏阴性菌中该DnaK ATP酶结构域片段对于DnaK伴侣蛋白系统具有进化意义。
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