DELINEATING THE MECHANISMS OF POLARITY IN BACTERIA AND RIBOSOME ASSEMBLY

描述细菌和核糖体组装的极性机制

基本信息

批准号：
7602892
负责人：
Janine R. Maddock
金额：
$ 2.33万
依托单位：
UNIVERSITY OF MICHIGAN AT ANN ARBOR
依托单位国家：
美国
项目类别：
财政年份：
2007
资助国家：
美国
起止时间：
2007-08-01 至 2008-07-31
项目状态：
已结题

项目摘要

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. It has been clearly established that proper function and regulation of many eukaryotic proteins and protein complexes require specific subcellular localization. Recent studies have demonstrated that many bacterial proteins are also sequestered to distinct cellular locations. Specifically, a number of chemotaxis, partitioning, cell division, and regulatory proteins in Escherichia coli, Caulobacter crescentus, and Bacillus subtilis, have been shown to be preferentially localized to the cell poles (for review see Lybarger and Maddock, 2001). These studies suggest that the ends of the bacterial cell provide a unique microenvironment, distinct from the rest of the cell, and demonstrate that organization of the bacterial cell is highly complex. One of our long-term goals is to assign a biological role to the clustering of chemoreceptors in bacteria and to assign clustering a biological role. By describing the function of chemoreceptor clustering in a well-characterized and genetically amenable model system like E. coli, we can quickly and conclusively answer some very specific but widely applicable questions. Moreover, relative to the majority of motile bacteria that contain large numbers of chemotaxis genes, E. coli represents a stream-lined cell with a simple chemotaxis system. Thus, by studying chemoreceptor localization in E. coli we can establish the rules that will certainly apply, at least in part, to other systems. A second long-term goal is to understand the nature of the polar microenvironment. To date, we have primarily focused on studies in E. coli and in the developmental bacterium, C. crescentus. With the completion of several bacterial genomes, it is now possible to catalog and examine polar proteins using proteomic tools. Parallel studies will be carried out in several bacteria to identify similarities and differences in the polar environments. The results of these studies will provide for a global picture of the bacterial cell pole. The bacterial ribosome is an extremely complicated macromolecular complex whose in vivo biogenesis is poorly understood. Although several bona fide assembly factors have been identified, their precise functions and temporal relationships are not clearly defined.

该副本是利用众多研究子项目之一由NIH/NCRR资助的中心赠款提供的资源。子弹和调查员（PI）可能已经从其他NIH来源获得了主要资金，因此可以在其他清晰的条目中代表。列出的机构是对于中心，这不一定是调查员的机构。已经确定，许多真核蛋白和蛋白质复合物的适当功能和调节需要特定的亚细胞定位。最近的研究表明，许多细菌蛋白也被隔离为不同的细胞位置。具体而言，大肠杆菌，花椰菜齿状细胞和枯草芽孢杆菌中的许多趋化性，分配，细胞分裂和调节蛋白被证明已被证明是优先定位于细胞杆的（有关综述，请参见Lybarger和Maddock，Maddock和Maddock，2001）。这些研究表明，细菌细胞的末端提供了独特的微环境，与细胞的其余部分不同，并证明细菌细胞的组织非常复杂。我们的长期目标之一是为化学感受器在细菌中的聚类中分配生物学作用，并分配聚类的生物学作用。通过描述化学感受器聚类在诸如大肠杆菌之类的良好特征和遗传上的模型系统中的功能，我们可以快速并最终回答一些非常具体但广泛适用的问题。此外，相对于大多数含有大量趋化基因的运动细菌，大肠杆菌代表具有简单趋化系统的溪流细胞。因此，通过研究大肠杆菌中的化学感受器定位，我们可以建立肯定至少部分适用于其他系统的规则。第二个长期目标是了解极性微环境的性质。迄今为止，我们主要专注于大肠杆菌和发育细菌的研究。随着几种细菌基因组的完成，现在可以使用蛋白质组学工具进行分类和检查极性蛋白质。平行研究将在几种细菌中进行，以确定极地环境中的相似性和差异。这些研究的结果将提供细菌细胞极的全球图像。细菌核糖体是一种极其复杂的大分子复合物，其体内生物发生知之甚少。尽管已经确定了几个真正的装配因素，但它们的确切功能和时间关系并未明确定义。