THE RESPONSE REGULATOR-LIKE DOMAIN OF RSSB

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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.