Biophysics, BIOTEC, Dresden University of Technology, Dresden, Germany.
Annu Rev Biophys. 2011;40:315-36. doi: 10.1146/annurev-biophys-042910-155332.
One of the most fundamental features of biological systems is probably their ability to self-organize in space and time on different scales. Despite many elaborate theoretical models of how molecular self-organization can come about, only a few experimental systems of biological origin have so far been rigorously described, due mostly to their inherent complexity. The most promising strategy of modern biophysics is thus to identify minimal biological systems showing self-organized emergent behavior. One of the best-understood examples of protein self-organization, which has recently been successfully reconstituted in vitro, is represented by the oscillations of the Min proteins in Escherichia coli. In this review, we summarize the current understanding of the mechanism of Min protein self-organization in vivo and in vitro. We discuss the potential of the Min oscillations to sense the geometry of the cell and suggest that spontaneous protein waves could be a general means of intracellular organization. We hypothesize that cooperative membrane binding and unbinding, e.g., as an energy-dependent switch, may act as an important regulatory mechanism for protein oscillations and pattern formation in the cell.
生物系统最基本的特征之一可能是它们在不同尺度上在空间和时间上自我组织的能力。尽管有许多关于分子自组织如何产生的精细理论模型，但由于其内在的复杂性，迄今为止只有少数具有生物起源的实验系统得到了严格描述。现代生物物理学最有前途的策略因此是确定显示自组织突现行为的最小生物系统。蛋白质自组织的一个最好理解的例子是大肠杆菌中 Min 蛋白的振荡，最近已成功在体外重建。在这篇综述中，我们总结了 Min 蛋白在体内和体外自我组织的机制的最新理解。我们讨论了 Min 振荡感知细胞几何形状的潜力，并提出自发的蛋白质波可能是细胞内组织的一般手段。我们假设膜结合和脱附的协同作用，例如作为能量依赖性开关，可能是细胞中蛋白质振荡和模式形成的重要调节机制。
