Stabilization of SecA ATPase by the primary cytoplasmic salt of Escherichia coli.
Stabilization of SecA ATPase by the primary cytoplasmic salt of Escherichia coli.
复制标题
大肠杆菌初级胞质盐对 SecA ATP 酶的稳定作用。
DOI：
10.1002/pro.3619
复制
发表时间：
2019
期刊：
影响因子：
--
通讯作者：
White,StephenH
中科院分区：
文献类型：
--
作者：
Roussel,Guillaume;Lindner,Eric;White,StephenH
许多人都知道赛卡马达ATPase的结构、功能和稳定性，它推动着周质蛋白在大肠杆菌内膜上的分泌。大多数对SecA的研究都是在缓冲的钠盐或氯化钾盐溶液中进行的。然而，主要的胞内盐E。大肠杆菌谷氨酸钾(KGlu)，它可以稳定折叠的蛋白质和蛋白质-核酸复合体。在这里，我们报告了KGlu稳定SecA，包括它的二聚体状态，并增加其ATPase活性，表明SecA可能完全折叠，稳定，并在37℃下活动。此外，KGlu还稳定分泌的麦芽糖结合蛋白的前体形式。
Much is known about the structure, function, and stability of the SecA motor ATPase that powers the secretion of periplasmic proteins across the inner membrane ofEscherichia coli. Most studies of SecA are carried out in buffered sodium or potassium chloride salt solutions. However, the principal intracellular salt ofE. coliis potassium glutamate (KGlu), which is known to stabilize folded proteins and protein‐nucleic acid complexes. Here we report that KGlu stabilizes SecA, including its dimeric state, and increases its ATPase activity, suggesting that SecA is likely fully folded, stable, and activein vivoat 37°C. Furthermore, KGlu also stabilizes a precursor form of the secreted maltose‐binding protein.