1887

Abstract

The expression of bacterial cold-shock proteins (CSPs) is highly induced in response to cold shock, and some CSPs are essential for cells to resume growth at low temperature. encodes five CSPs (named CspA to CspE) with significant amino acid homology to CspA of . In contrast to , the insertional knock-out of a single gene () strongly affected growth of independent of temperature. In the case of three of the genes (, , ) more than one specific transcript could be detected. The net amount of , and transcripts increased strongly after cold shock, while no such effect could be observed for and . The exposure to other stress conditions, including translation inhibitors, heat shock, osmotic stress and nutrient deprivation in the stationary phase, indicated that the genes are also responsive to these conditions. The coding regions of all of the cold-shock genes are preceded by a long non-translated upstream region (5′-UTR). In the case of the gene, a deletion of parts of this region led to a significant reduction of translation of the resulting truncated transcript, indicating a role of the 5′-UTR in translational control. The cold-shock stimulon was investigated by 2D-PAGE and mass spectrometric characterization, leading to the identification of additional cold-inducible proteins (CIPs). Interestingly, two cold-shock genes ( and ) were found to be under the negative control of the BvgAS system, the main transcriptional regulator of virulence genes. Moreover, a negative effect of slight overexpression of CspB, but not of the other CSPs, on the transcription of the adenylate cyclase toxin CyaA of was observed, suggesting cross-talk between the CSP-mediated stress response stimulon and the virulence regulon.

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2005-06-01
2020-04-09
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