Amino Acid Repair Activity in Helicobacter pylori

性状（由申请方提供）：甲硫氨酸亚砜还原酶（Msr's）催化甲硫氨酸亚砜还原为（正常）甲硫氨酸。结果是氧化损伤蛋白的再活化，已知这种活性有助于H.幽门。本项目旨在鉴定与三种已鉴定的H相关的关键氨基酸残基。pylori蛋白进行这种还原修复过程。将鉴定两种类型的功能残基。这些是由Msr修复的特异性Met残基，以及参与识别Msr的残基。关键类型的残基将通过研究纯H。pylori Msr及其与鉴定的靶蛋白的相互作用。来自纯蛋白研究的信息将用于评估全细胞暴露于应激剂后靶蛋白中氧化性Met残基损伤的程度。然后，关于单个靶蛋白对接位点（Msr相互作用位点）的信息将用于理解H中每个靶蛋白修复的需要。pylori应激生理和胃定植能力。公共卫生相关性：由持续存在的人类病原体幽门螺杆菌进行的甲硫氨酸修复对于细菌在胃中的生存至关重要。用于修复富含甲硫氨酸的蛋白质的机制和这种修复的生理后果将被揭示，以便可以开发对抗病原体的措施。

DESCRIPTION (provided by applicant): Methionine sulfoxide reductases (Msr's) catalyze the reduction of methionine sulfoxide back to (normal) methionine. The result is reactivation of oxidatively damaged proteins and this activity is known to facilitate successful gastric colonization by H. pylori. This project is designed to identify the critical amino acid residues associated with three identified H. pylori proteins that undergo this reductive repair process. Two types of functional residues will be identified. These are the specific Met residues repaired by Msr, and the residues involved in recognizing Msr. The key types of residues will be identified by studying pure H. pylori Msr and its interaction with identified target proteins. The information from the pure protein studies will be used to assess the degree of oxidative Met residue damage in the target proteins upon stress agent exposure of whole cells. Then the information on the individual target proteins docking sites (Msr-interacting sites) will be used to understand the need for each target proteins repair in H. pylori stress physiology and stomach colonizing abilities. PUBLIC HEALTH RELEVANCE: Methionine repair by the persistent human pathogen Helicobacter pylori is important for the bacterium to survive in the stomach. The mechanisms used to repair methionine-rich proteins and the physiological consequences of such repair will be uncovered so that measures to counteract the pathogen can be developed.