High pressure inhibits signaling protein binding to the flagellar motor and bacterial chemotaxis through enhanced hydration
High pressure inhibits signaling protein binding to the flagellar motor and bacterial chemotaxis through enhanced hydration
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DOI：
10.1038/s41598-020-59172-3
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发表时间：
2020-02-11
影响因子：
4.6
通讯作者：
Kitao, Akio
中科院分区：
文献类型：
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作者：
Hata, Hiroaki;Nishihara, Yasutaka;Kitao, Akio
低于100mpa的高压会干扰分子间的相互作用，但不会引起蛋白质的压力变性。在大肠杆菌中，趋化信号蛋白CheY与鞭毛运动蛋白FliM的结合诱导了运动旋转的逆转。利用分子动力学（MD）模拟和平行级联选择MD (PaCS-MD)，我们发现高压增加了CheY第一水化壳中的水密度，并在很大程度上诱导水渗透到CheY- flim界面。PaCS-MD使我们能够在原子分辨率下观察到CheY-FliM配合物的压力诱导解离。结合自由能的压力依赖性表明，当压力从0.1 MPa增加到100 MPa时，结合明显减弱。使用高压显微镜，我们观察到高静水压力固定电机旋转逆时针方向。综上所述，施加压力增强了蛋白质的水合作用，减弱了CheY与FliM的结合，阻止了鞭毛运动的逆转。
High pressure below 100 MPa interferes inter-molecular interactions without causing pressure denaturation of proteins. In Escherichia coli, the binding of the chemotaxis signaling protein CheY to the flagellar motor protein FliM induces reversal of the motor rotation. Using molecular dynamics (MD) simulations and parallel cascade selection MD (PaCS-MD), we show that high pressure increases the water density in the first hydration shell of CheY and considerably induces water penetration into the CheY-FliM interface. PaCS-MD enabled us to observe pressure-induced dissociation of the CheY-FliM complex at atomic resolution. Pressure dependence of binding free energy indicates that the increase of pressure from 0.1 to 100 MPa significantly weakens the binding. Using high-pressure microscopy, we observed that high hydrostatic pressure fixes the motor rotation to the counter-clockwise direction. In conclusion, the application of pressure enhances hydration of the proteins and weakens the binding of CheY to FliM, preventing reversal of the flagellar motor.