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Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins

机译:细菌细胞分裂蛋白形成相互转换动态模式的多种模式

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Min proteins of the Escherichia coli cell division system oscillate between the cell poles in vivo. In vitro on a solid-surface supported lipid bilayer, these proteins exhibit a number of interconverting modes of collective ATP-driven dynamic pattern formation including not only the previously described propagating waves, but also near uniformity in space surface concentration oscillation, propagating filament like structures with a leading head and decaying tail and moving and dividing amoeba-like structures with sharp edges. We demonstrate that the last behavior most closely resembles in vivo system behavior. The simple reaction-diffusion models previously proposed for the Min system fail to explain the results of the in vitro self-organization experiments. We propose the hypotheses that initiation of MinD binding to the surface is controlled by counteraction of initiation and dissociation complexes; the binding of MinD/E is stimulated by MinE and involves polymerization-depolymerization dynamics; polymerization of MinE over MinD oligomers triggers dynamic instability leading to detachment from the membrane. The physical properties of the lipid bilayer are likely to be one of the critical determinants of certain aspects of the dynamic patterns observed.
机译:大肠杆菌细胞分裂系统的最小蛋白质在体内细胞极之间振荡。在体外的固体表面支持的脂质双层上,这些蛋白表现出多种相互转换的集体ATP驱动的动态模式形成模式,不仅包括先前描述的传播波,而且空间表面浓度振荡几乎均一,传播了丝状结构头部前导,尾巴腐烂,移动和分开的变形虫状结构,边缘锋利。我们证明最后的行为与体内系统行为最相似。先前为Min系统提出的简单反应扩散模型无法解释体外自组织实验的结果。我们提出的假设是,MinD结合到表面的起始受起始和离解复合物的反作用控制。 MinD / E的结合受MinE刺激,并涉及聚合-解聚动力学。 MinE在MinD低聚物上的聚合会引发动态不稳定性,从而导致其从膜上脱离。脂质双层的物理性质可能是观察到的动态模式某些方面的关键决定因素之一。

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