The general stress response provides a pathway for bacteria to survive in response to a range of different environmental stresses. This pathway is largely controlled at the post-translational level through the regulated degradation of the transcription factor, SigmaS (σ^S). Under normal conditions, the phosphorylated adaptor protein RssB recognises σ^S and delivers it to the ClpXP protease where it is rapidly degraded. In contrast, under conditions of “general” stress the turnover of σ^S is inhibited by a number of stress-specific anti-adaptors, which as the name suggests inhibit the activity of the adaptor protein, RssB. Currently however, the molecular details of the steps which lead to, or prevent, σ^S turnover are poorly defined. Here we describe our current understanding of the molecular details of this process. Using a range of biochemical assays we have identified not only the mechanism by which σ^S is recognised by RssB and delivered to ClpXP for degradation, but also the molecular details of the interaction between RssB and the various anti-adaptor proteins, which prevent its delivery. Collectively, these data improve our understanding of σ^S turnover and the general stress response.