Differential induction of heat shock, SOS, and oxidation stress regulons and accumulation of nucleotides in Escherichia coli

Abstract

Heat and various inhibitory chemicals were tested in Escherichia coli for the ability to cause accumulationi of adenylylated nucleotides and to induce proteins of the heat shock (htpR-controlled), the oxidation stress (oxyR-controlled), and the SOS (lexA-controlled) regdlons. Under the conditions used, heat and ethanol initiated solely a heat shock response, hydrogen peroxide and 6-amino7-chloro-5,8-dioxoquinoline (ACDQ) induced primarily an oxidation stress response and secondaily an SOS response, nalidixic acid and puromycin induced primarily an SOS and secondarily a heat shock response, isoleucine restriction induced a poor heat shock response, and CdCI2 strongly induced all three stress responses. ACDQ, CdCl2, and H202 each stimulated the synthesis of approximately 35 proteins by factors of 5-to 50-fold, and the heat shock, oxidation stress, and SOS regulons constituted a minor fraction of the overall cellular response. The pattern of accumulation of adenylylated nucleotides during these treatments was inconsistent with a simple role for these nucleotides as alarmones sufficient for triggering the heat shock response, but was consistent with a role in the oxyRlmediated response.

Yersinia enterocolitica immunodominant 60 kDa antigen, common to a broad range of bacteria, is a heat-shock protein

“…enterocolitica. In E. coli, there is a set of 17 heat shock proteins, one of which is the GroEL protein (Neidhardt et al, 1984;VanBogelen et al, 1987). The fact that CRPA is found in the same relative migratory position in two-dimensional gels as the GroEL protein of E. coli, coupled with the fact that the native molecular mass of both proteins is > 500 kDa, suggested to us that they might be similar or identical proteins (Hendrix, 1979).…”

Quantifying changes in the thiol redox proteome upon oxidative stress in vivo

“…5 in SI Appendix). Similar concentrations of H 2 O 2 , for instance, have been used in earlier proteomic studies designed to investigate the E. coli oxidative stress response (28). To detect proteins that are rapidly oxidatively modified in vivo, we then harvested cells 10 min after addition of the oxidants and conducted our OxICAT thiol trapping experiments.…”

The induction of oxidative enzymes in Streptomyces coelicolor upon hydrogen peroxide treatment

“…The genes induced by H202 include katG, ahpC, ahpF and gorA, and are all controlled by the positive regulator OxyR (Christman et al, 1985(Christman et al, , 1989Morgan et al, 1986). The so-called soxR and oxyR regulons seem to overlap other stress response regulons such as that for heat-shock, since some proteins are induced in common by different stresses (Greenberg & Demple, 1989;VanBogelen et al, 1987), and some cross-protection has been observed (Christman et al, 1985;Jenkins et al, 1988).…”