Anti-adaptors use distinct modes of binding to inhibit the RssB-dependent turnover of RpoS (σ(S)) by ClpXP.

ABSTRACT: In Escherichia coli, σ(S) is the master regulator of the general stress response. The level of σ(S) changes in response to multiple stress conditions and it is regulated at many levels including protein turnover. In the absence of stress, σ(S) is rapidly degraded by the AAA+ protease, ClpXP in a regulated manner that depends on the adaptor protein RssB. This two-component response regulator mediates the recognition of σ(S) and its delivery to ClpXP. The turnover of σ(S) however, can be inhibited in a stress specific manner, by one of three anti-adaptor proteins. Each anti-adaptor binds to RssB and inhibits its activity, but how this is achieved is not fully understood at a molecular level. Here, we describe details of the interaction between each anti-adaptor and RssB that leads to the sta

SUBMITTER: Micevski D 

PROVIDER: S-EPMC4428439 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature