Repair of methionine residues in H. pylori catalase

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。这个重点项目的目的是确定与一个确定的H相关的关键氨基酸残基。幽门螺杆菌蛋白（过氧化氢酶）经历这种还原修复过程。鉴定由Msr修复的特定Met残基是最直接的兴趣。将通过研究纯H来鉴定残留物。pylori Msr及其与纯过氧化氢酶的相互作用。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所承受的氧化性Met残基损伤程度。拟议的项目是一个小型的自给自足的一个非常成功的病原体。公共卫生相关性：细菌对氨基酸（蛋氨酸）的修复，导致消化性溃疡和胃癌，对于病原体在宿主中的生存至关重要。建议了解哪些因素影响关键蛋白质中这种修复的需要。

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 focused project is designed to identify the critical amino acid residues associated with one identified H. pylori protein (catalase) that undergoes this reductive repair process. Identification of the specific Met residues repaired by Msr is of the most immediate interest. The residues will be identified by studying pure H. pylori Msr and its interaction with pure catalase. The information from the pure protein studies will be used to assess the degree of oxidative Met residue damage the target protein sustains upon stress agent exposure of whole cells. The proposed project is a small self-contained one on a highly successful pathogen. PUBLIC HEALTH RELEVANCE: The repair of an amino acid (methionine) by a bacterium that causes peptic ulcers and gastric cancers is important for the pathogens survival in the host. It is proposed to understand what factors influence the need for this repair in a key protein.