A Molecular Study of Min-Protein Polymer Dynamics

最小蛋白聚合物动力学的分子研究

• 批准号: 7478728
• 负责人: KERWYN C. HUANG
• 金额: $ 12.28万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2005
• 资助国家: 美国
• 起止时间: 2005-08-01 至 2010-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7478728
• 关键词: Bacteria; Biology; Cell Shape; Cell division; Cells; Computer Simulation; Data Quality; Development; Diffusion; Escherichia coli; Eukaryota; Eukaryotic Cell; Goals; Green Fluorescent Proteins; In Vitro; Individual; Lead; Location; Measures; Membrane; Methods; Mind; Mining; Modeling; Molecular; Neisseria gonorrhoeae; Nucleotides; Numbers; Pattern; Polymers; Process; Prokaryotic Cells; Property; Proteins; Range; Rate; Reaction; Research; Resources; Role; Role playing therapy; Scientist; Shapes; Structure; System; Time; Training; Universities; Work; cell motility; density; in vivo; numb protein; particle; prevent; promoter; research study; retinal rods; simulation; size

DESCRIPTION (provided by applicant): The remarkable accuracy of cell division in E. coli and related bacteria is partially regulated by the Minprotein system, which prevents division near the cell ends by oscillating spatially from pole to pole. The scientist has recently developed a complete model of the Min system, using only known properties of the proteins, which accurately reproduces the observed oscillations and predicts a finite nucleotide exchange rate for the MinD protein of around one second, a number that has since been experimentally verified to a high degree of accuracy. This proposal concerns efforts to develop particle-level simulations in rod-shaped cells, to capture for the first time the helical polymer dynamics of the Min proteins. In addition, the scientist intends to extend the model to round cells, to determine whether Min oscillations can spontaneously select the long axis of the cell to define the division plane in cocci in the presence of statistical fluctuations. These particle-level simulations provides a starting point for a general understanding of how prokaryotes and eukaryotes can use a reaction-diffusion protein system to target proteins to different locations and to detect their own geometry, and will have broad applications at the expanding interface between large-scale computation and the microscale biology of protein interactions. In order to understand the mechanism behind E. coli's incredible division accuracy, the scientist will undertake experiments incorporating computational results to study the effects of changes in concentration on oscillation period and division accuracy. The theoretical work will be performed in Dr. Ned Wingreen's lab at Princeton University, with experimental resources and training provided by Dr. Bonnie Bassler at Princeton University.

描述（由申请人提供）：E.大肠杆菌和相关细菌的细胞分裂部分受到Minprotein系统的调节，该系统通过在两极之间进行空间振荡来防止细胞末端附近的分裂。这位科学家最近开发了一个完整的Min系统模型，只使用蛋白质的已知特性，准确地再现了观察到的振荡，并预测了MinD蛋白质的有限核苷酸交换率约为一秒，这个数字已经被实验验证到高度的准确性。这项建议涉及的努力，开发粒子级模拟杆状细胞，捕捉第一次的螺旋聚合物动力学的Min蛋白质。此外，科学家打算将该模型扩展到圆形细胞，以确定Min振荡是否可以自发地选择细胞的长轴，以在统计波动的存在下定义球菌中的分裂平面。这些粒子级的模拟提供了一个起点，为原核生物和真核生物如何使用反应扩散蛋白质系统的目标蛋白质到不同的位置，并检测自己的几何形状的一般理解，并将有广泛的应用在大规模计算和蛋白质相互作用的微观生物学之间的扩展接口。为了了解E.由于大肠杆菌的分裂精确度令人难以置信，科学家将进行实验，结合计算结果，研究浓度变化对振荡周期和分裂精确度的影响。理论工作将在普林斯顿大学Ned Wingreen博士的实验室进行，由普林斯顿大学Bonnie Bassler博士提供实验资源和培训。