Discovery and characterization of new bacterial cell division genes

新细菌细胞分裂基因的发现和表征

• 批准号: 7932510
• 负责人: DAVID S WEISS
• 金额: $ 6万
• 依托单位: UNIVERSITY OF IOWA
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-09-30 至 2010-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7932510
• 关键词: Amino Acids; Animal Model; Antibiotics; Bacteria; Binding; Binding Sites; Biochemical; Biochemistry; Biological Assay; Calorimetry; Cell division; Cells; Cleaved cell; Collection; Communities; Complex; Cytoplasmic Tail; Development; Ensure; Escherichia coli; Future; Genes; Goals; Knowledge; Lead; Mediating; Membrane; Metabolism; Methods; Modeling; Peptidoglycan; Phenotype; Play; Polysaccharides; Proteins; Public Health; Role; Signal Transduction; Site; Site-Directed Mutagenesis; Solutions; Structure; System; Tertiary Protein Structure; Testing; Titrations; Transmission Electron Microscopy; base; cell envelope; constriction; design; follow-up; improved; in vivo; insight; mutant; novel; protein protein interaction; protein structure; public health relevance; research study; structural biology; yeast two hybrid system

DESCRIPTION (provided by applicant): The long-term goal of these studies is to better understand cell division in the model organism Escherichia coli. A deeper understanding of bacterial cell division is expected to facilitate the development of new antibiotics and will therefore benefit public health. In E. coli, cell division is mediated by a structure called the "septal ring," which is known to contain about 20 proteins. An important challenge for the future will be to identify and characterize any proteins that are missing from the current model. The experiments proposed here concern three newly discovered E. coli septal ring proteins that carry a peptidoglycan binding domain known as a SPOR domain. Specific Aim1 will explore the roles of the SPOR domain proteins during constriction. Specific Aims 2 and 3 are based on the observation that the SPOR domains themselves localize to the division site. This implies that SPOR domains bind preferentially to septal peptidoglycan. Aim 2 explores structural features of peptidoglycan that are recognized by SPOR domains. Aim 3 defines the structure of the peptidoglycan binding site on a SPOR domain. Understanding how SPOR domains specifically target septal peptidoglycan might provide important insights into septal peptidoglycan synthesis. PUBLIC HEALTH RELEVANCE: The studies proposed here will lead to a greater understanding of bacterial cell division. That knowledge can be used to develop new antibiotics.

描述（由申请方提供）：这些研究的长期目标是更好地了解模式生物大肠杆菌中的细胞分裂。对细菌细胞分裂的更深入了解有望促进新抗生素的开发，从而有益于公众健康。在大肠在大肠杆菌中，细胞分裂是由一种称为“隔环”的结构介导的，已知该结构含有约20种蛋白质。未来的一个重要挑战将是识别和表征当前模型中缺失的任何蛋白质。本文提出的实验涉及三个新发现的E.大肠杆菌隔环蛋白，携带称为SPOR结构域的肽聚糖结合域。特异性Aim1将探索收缩过程中SPOR结构域蛋白的作用。具体目的2和3基于SPOR结构域自身定位于分裂位点的观察。这意味着SPOR结构域优先结合间隔肽聚糖。目的2探索SPOR结构域识别的肽聚糖的结构特征。目的3定义了SPOR结构域上肽聚糖结合位点的结构。了解SPOR结构域如何特异性靶向隔肽聚糖可能为隔肽聚糖合成提供重要见解。公共卫生相关性：这里提出的研究将导致对细菌细胞分裂的更好理解。这些知识可以用来开发新的抗生素。