Min protein patterns emerge from rapid rebinding and membrane interaction of MinE
Min protein patterns emerge from rapid rebinding and membrane interaction of MinE
复制标题
DOI：
10.1038/nsmb.2037
复制
发表时间：
2011-05-01
影响因子：
16.8
通讯作者：
Schwille, Petra
中科院分区：
文献类型：
--
作者：
Loose, Martin;Fischer-Friedrich, Elisabeth;Schwille, Petra
在大肠杆菌中，Min蛋白质的极到极振荡指导隔膜形成到中细胞，这是对称细胞分裂所必需的。在体外，蛋白质波来自MinD（一种膜结合ATP酶）及其激活剂MinE的自组织。对于波的传播，蛋白质需要通过集体膜结合和解除结合的状态循环。虽然MinD可能经历合作膜附着，但尚不清楚同步脱离是如何协调的。我们使用共聚焦和单分子显微镜来阐明Min波传播过程中的事件顺序。我们建议，蛋白质脱离波的后部，和E环的形成，是由两个互补的过程完成的：第一，局部积累的MinE由于快速重新绑定，导致动态不稳定性;和第二，结构变化引起的膜相互作用的MinE在一个等摩尔的MinD-MinE（MinDE）复杂的，这支持了图案形成的鲁棒性。
In Escherichia coli, the pole-to-pole oscillation of the Min proteins directs septum formation to midcell, which is required for symmetric cell division. In vitro, protein waves emerge from the self-organization of MinD, a membrane-binding ATPase, and its activator MinE. For wave propagation, the proteins need to cycle through states of collective membrane binding and unbinding. Although MinD presumably undergoes cooperative membrane attachment, it is unclear how synchronous detachment is coordinated. We used confocal and single-molecule microscopy to elucidate the order of events during Min wave propagation. We propose that protein detachment at the rear of the wave, and the formation of the E-ring, are accomplished by two complementary processes: first, local accumulation of MinE due to rapid rebinding, leading to dynamic instability; and second, a structural change induced by membrane-interaction of MinE in an equimolar MinD-MinE (MinDE) complex, which supports the robustness of pattern formation.