STRUCTURE DETERMINATION OF E COLI HSP33, REDOX SENSITIVE CHAPERONE

Hsp 33是一种新的高度保守的热休克蛋白 E.杆菌 Jakob博士在Dr. Bardwell的实验室表明，Hsp 33是一种非常有效的 分子伴侣在保护未折叠蛋白质免受不可逆 聚合来 根据环境的氧化还原状态，Hsp 33 伴侣活性是开启或关闭的。 正常还原下 条件下，Hsp 33是不活跃的;然而，Hsp 33变成了活跃的 当暴露于氧化应激时折叠辅助蛋白。 这是一 已知由人类吞噬细胞诱导的应激， 杀死入侵生物的防御。 体内实验支持 我们的体外研究结果显示，热休克蛋白33是一个重要的球员， 保护原核生物免受氧化应激。 我们有兴趣 寻找这种新型氧化还原敏感的结构机制， HSP 33的分子伴侣功能。

Hsp33 is a member of a new and highly conserved heat shock protein family in E. coli. In vitro experiments by Dr. Jakob in Dr. Bardwell's laboratory reveal that Hsp33 is an extremely efficient molecular chaperone in protecting unfolding proteins from irreversible aggregation. Depending on the redox state of the environment, Hsp33's chaperone activity is either on or off. Under normal reducing conditions, Hsp33 is inactive; however, Hsp33 turns into an active folding helper protein when exposed to oxidative stress. This is a stress known to be induced by human phagocytes, the first line of defense in killing invading organisms. In vivo experiments support our in vitro findings by revealing that Hsp33 is an important player in protecting prokaryotes from oxidative stress. We are interested in finding the structural mechanism of this novel redox sensitive chaperone function of HSP33.