THE RESPONSE REGULATOR-LIKE DOMAIN OF RSSB

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 RSSB是一种调节蛋白，与大肠杆菌中的应激反应有关。它在其N-末端结构域的Asp57处被ArcB组氨酸激酶磷酸化。在RSSB的磷酸化过程中，它与RNA聚合酶调节亚基Sigma-S结合，并靶向Sigma-S被ClpXP降解。以其非磷酸化形式，RSSB不结合Sigma-S，允许Sigma-S通过启动稳定期和胁迫反应基因来积累和发挥其作用。我们有兴趣了解RSSB与Sigma-S、激酶和ClpX相互作用的结构基础。

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. RssB is a regulatory protein involved in the stress response in E. coli. It is phosphorylated at Asp57 of its N-terminal domain by the ArcB histidine kinase. In its phosphorylated from RssB binds to sigma-S regulatory subunit of RNA polymerase and targets sigma-S for degradation by ClpXP. In its non- phosphorylated form RssB does not bind sigma-S, allowing sigma-S to accumulate and exert its effect by turning on stationary phase and stress response genes. We are interested in understanding the structural basis for the interaction of RssB with sigma-S, the kinase, and ClpX.