Theoretische Physik, Universität des Saarlandes, Saarbrücken, Germany.
PLoS Comput Biol. 2013;9(12):e1003347. doi: 10.1371/journal.pcbi.1003347. Epub 2013 Dec 5.
The rod-shaped bacterium Escherichia coli selects the cell center as site of division with the help of the proteins MinC, MinD, and MinE. This protein system collectively oscillates between the two cell poles by alternately binding to the membrane in one of the two cell halves. This dynamic behavior, which emerges from the interaction of the ATPase MinD and its activator MinE on the cell membrane, has become a paradigm for protein self-organization. Recently, it has been found that not only the binding of MinD to the membrane, but also interactions of MinE with the membrane contribute to Min-protein self-organization. Here, we show that by accounting for this finding in a computational model, we can comprehensively describe all observed Min-protein patterns in vivo and in vitro. Furthermore, by varying the system's geometry, our computations predict patterns that have not yet been reported. We confirm these predictions experimentally.
杆状细菌大肠杆菌在 MinC、MinD 和 MinE 蛋白的帮助下选择细胞中心作为分裂部位。该蛋白系统通过在两个细胞半体之一的膜上交替结合来在两个细胞极之间交替振荡。这种动态行为源于细胞膜上 ATPase MinD 及其激活剂 MinE 的相互作用，已成为蛋白质自我组织的范例。最近，人们发现，不仅 MinD 与膜的结合，而且 MinE 与膜的相互作用都有助于 Min 蛋白的自我组织。在这里，我们通过在计算模型中考虑这一发现，全面描述了所有观察到的体内和体外 Min 蛋白模式。此外，通过改变系统的几何形状，我们的计算预测了尚未报道的模式。我们通过实验证实了这些预测。
