Insight into the RssB-Mediated Recognition and Delivery of σ^s to the AAA+ Protease, ClpXP.

ABSTRACT: In Escherichia coli, SigmaS (σ^S) is the master regulator of the general stress response. The cellular levels of σ^S are controlled by transcription, translation and protein stability. The turnover of σ^S, by the AAA+ protease (ClpXP), is tightly regulated by a dedicated adaptor protein, termed RssB (Regulator of Sigma S protein B)-which is an atypical member of the response regulator (RR) family. Currently however, the molecular mechanism of σ^S recognition and delivery by RssB is only poorly understood. Here we describe the crystal structures of both RssB domains (RssB_N and RssB_C) and the SAXS analysis of full-length RssB (both free and in complex with σ^S). Together with our biochemical analysis we propose a

SUBMITTER: Micevski D 

PROVIDER: S-EPMC7226468 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature