Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli.

ABSTRACT: All cells must adapt to rapidly changing conditions. The heat shock response (HSR) is an intracellular signaling pathway that maintains proteostasis (protein folding homeostasis), a process critical for survival in all organisms exposed to heat stress or other conditions that alter the folding of the proteome. Yet despite decades of study, the circuitry described for responding to altered protein status in the best-studied bacterium, E. coli, does not faithfully recapitulate the range of cellular responses in response to this stress. Here, we report the discovery of the missing link. Surprisingly, we found that σ(32), the central transcription factor driving the HSR, must be localized to the membrane rather than dispersed in the cytoplasm as previously assumed. Genetic analyses indicate th

SUBMITTER: Lim B 

PROVIDER: S-EPMC3866087 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature