Abstract
The general stress response in Escherichia coli is activated by several stress agents, including entering the stationary growth phase. This response constitutes a complex regulatory network in which a large number of genes are induced and others are repressed. The stress response is regulated by the alternative sigma factor σ(S) encoded by the rpoS gene. The rpoS transcripts are substrates of the RNA binding protein, Hfq, which is essential for its translation. The rpoS mRNA is also a substrate of the cold shock protein C (CspC) which stabilizes the transcripts. Here we demonstrate, using pull-down assays, that CspC interacts with Hfq via mRNA molecules. We also show that CspC acts on the 5' UTR of the rpoS transcript, but its activity on rpoS is independent of Hfq. Moreover, we show that CspC suppresses the phenotypes of an hfq deletion. These results elucidate a new aspect in the post-transcriptional regulation of the stress response and will further our understanding of this complex network.
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