Institute for Solid State Physics, University of Tokyo, Kashiwa, Chiba, 277-8581, Japan.
Sci Rep. 2019 Aug 13;9(1):11721. doi: 10.1038/s41598-019-48102-7.
Proteins often form chiral assembly structures on a biomembrane. However, the role of the chirality in the interaction with an achiral membrane is poorly understood. Here, we report how chirality of crescent-shaped protein rods changes their assembly and tubulation using meshless membrane simulations. The achiral rods deformed the membrane tube into an elliptical shape by stabilizing the edges of the ellipse. In contrast, the chiral rods formed a helical assembly that generated a cylindrical membrane tube with a constant radius in addition to the elliptical tube. This helical assembly could be further stabilized by the direct side-to-side attraction between the protein rods. The chirality also promotes the tubulation from a flat membrane. These results agree with experimental findings of the constant radius of membrane tubules induced by the Bin/Amphiphysin/Rvs (BAR) superfamily proteins.
蛋白质经常在生物膜上形成手性组装结构。然而,手性在与非手性膜相互作用中的作用还不太清楚。在这里,我们报告了新月形蛋白棒的手性如何通过无网格膜模拟改变它们的组装和管状化。非手性棒通过稳定椭圆的边缘将膜管变形为椭圆形。相比之下,手性棒形成了螺旋组装,除了椭圆形管之外,还生成了具有恒定半径的圆柱形膜管。这种螺旋组装可以通过蛋白棒之间的直接侧向吸引力进一步稳定。手性还促进了从平面膜的管状化。这些结果与 Bin/Amphiphysin/Rvs (BAR) 超家族蛋白诱导的膜管恒定半径的实验结果一致。