Structure of phosphorylated-like RssB, the adaptor delivering σ^s to the ClpXP proteolytic machinery, reveals an interface switch for activation.

ABSTRACT: In enterobacteria such as Escherichia coli, the general stress response is mediated by σ^s, the stationary phase dissociable promoter specificity subunit of RNA polymerase. σ^s is degraded by ClpXP during active growth in a process dependent on the RssB adaptor, which is thought to be stimulated by the phosphorylation of a conserved aspartate in its N-terminal receiver domain. Here we present the crystal structure of full-length RssB bound to a beryllofluoride phosphomimic. Compared to the structure of RssB bound to the IraD anti-adaptor, our new RssB structure with bound beryllofluoride reveals conformational differences and coil-to-helix transitions in the C-terminal region of the RssB receiver domain and in the interdomain segmented helical linker. These are accompan

SUBMITTER: Brugger C 

PROVIDER: S-EPMC10755785 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature