Resistance to environmental stress requires the RNA chaperones CspC and CspE.

Stress response is essential for adaptation and for survival during environmental changes. A major factor in these responses is RpoS (σS), the master regulator of stationary phase and of the general stress response in Escherichia coli. RpoS is regulated by a complex network at several levels - transcription, translation and proteolysis. Previous studies indicated that rpoS transcripts are stabilized by overexpression of the cold shock proteins CspC and CspE. Here we demonstrate the importance of this transcript stabilization in the regulatory networks governing σS activity. We show that upon entry into stationary-phase rpoS transcripts are stabilized and this stabilization is necessary for the increased activity of σS. The increase in rpoS transcript stability requires at least one of the cold shock proteins CspC and CspE. We also show that the cellular concentration of CspC - but not CspE - increases concurrently with the increase in rpoS transcript stability, probably accounting for this stabilization. These data expand previous data showing that upon heat shock there is a reduction in CspC levels, coupled to a reduced half-life of heat shock gene transcripts. Taken together, it appears that CspC levels modulate transcript stability upon exposure to environmental stress while CspE acts as a 'housekeeping RNA chaperone' under general stress conditions.