Involvement of rppH in thermoregulation in Pseudomonas syringae

J Bacteriol. 2014 Jun;196(12):2313-22. doi: 10.1128/JB.00057-14. Epub 2014 Apr 11.


Temperature, among other environmental factors, influences the incidence and severity of many plant diseases. Likewise, numerous traits, including the expression of virulence factors, are regulated by temperature. Little is known about the underlying genetic determinants of thermoregulation in plant-pathogenic bacteria. Previously, we showed that the expression of both fliC (encoding flagellin) and syfA (encoding a nonribosomal polypeptide synthetase) was suppressed at high temperatures in Pseudomonas syringae. In this work, we used a high-throughput screen to identify mutations that conferred overexpression of syfA at elevated temperatures (28°C compared to 20°C). Two genes, Psyr_2474, encoding an acyl-coenzyme A (CoA) dehydrogenase, and Psyr_4843, encoding an ortholog of RppH, which in Escherichia coli mediates RNA turnover, contribute to thermoregulation of syfA. To assess the global role of rppH in thermoregulation in P. syringae, RNA sequencing was used to compare the transcriptomes of an rppH deletion mutant and the wild-type strain incubated at 20°C and 30°C. The disruption of rppH had a large effect on the temperature-dependent transcriptome of P. syringae, affecting the expression of 569 genes at either 20°C or 30°C but not at both temperatures. Intriguingly, RppH is involved in the thermoregulation of ribosome-associated proteins, as well as of RNase E, suggesting a prominent role of rppH on the proteome in addition to its effect on the transcriptome.

MeSH terms

  • Acid Anhydride Hydrolases / genetics
  • Acid Anhydride Hydrolases / metabolism*
  • Adaptation, Physiological / physiology*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Gene Deletion
  • Gene Expression Regulation, Bacterial / physiology*
  • Gene Expression Regulation, Enzymologic
  • Mutagenesis
  • Pseudomonas syringae / genetics
  • Pseudomonas syringae / metabolism*
  • Temperature


  • Bacterial Proteins
  • Acid Anhydride Hydrolases