Abstract
The rpoH gene encoding a heat shock sigma factor, σ32, was cloned from the psychrophilic bacterium Colwellia maris. The deduced amino acid sequence of σ32 from C. maris is more than 60% homologous to that of σ32 from mesophilic bacteria. The RpoH box, a 9-amino-acid sequence region (QRKLFFNLR) specific to σ32, and two downstream box sequences complementary to a part of 16S rRNA were identified. Primer extension analysis showed that the C. maris rpoH is expressed from only one σ70-type promoter. Northern blot analysis showed that the level of rpoH mRNA was clearly increased at 20°C, a temperature that induces heat shock in this organism. In the presence of an inhibitor of transcriptional initiation, the degradation of rpoH mRNA was much slower at 20°C than at 10°C. Thus, increased stability of the rpoH mRNA might be responsible for the rpoH mRNA accumulation. The predicted secondary structure of the 5′-region of C. maris rpoH mRNA was different from the conserved patterns reported for most mesophilic bacteria, and the base pairing of the downstream boxes appeared to be less stable than that of Escherichia coli rpoH mRNA. Thus, essential features that ensure the HSP expression at a relatively low temperature are embedded in the rpoH gene of psychrophiles.
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Acknowledgement
This work was supported in part by a Grant-in-Aid for Scientific Research (no. 15013243 to Y.N.) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.
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Communicated by K. Horikoshi
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Yamauchi, S., Okuyama, H., Nishiyama, Y. et al. The rpoH gene encoding heat shock sigma factor σ32 of psychrophilic bacterium Colwellia maris. Extremophiles 10, 149–158 (2006). https://doi.org/10.1007/s00792-005-0485-9
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DOI: https://doi.org/10.1007/s00792-005-0485-9