THE RESPONSE REGULATOR-LIKE DOMAIN OF RSSB

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。RssB是大肠杆菌中参与应激反应的调节蛋白。杆菌其N端结构域的Asp 57被ArcB组氨酸激酶磷酸化。在其磷酸化中，RssB与RNA聚合酶的σ-S调节亚基结合，并靶向σ-S以供ClpXP降解。在其非磷酸化形式中，RssB不结合σ-S，允许σ-S积累并通过开启稳定期和应激反应基因发挥其作用。我们感兴趣的是了解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.