Regulation of superoxide stress in Pseudomonas putida KT2440 is different from the SoxR paradigm in Escherichia coli

Woojun Park, Samuel Peña-Llopis, Yunho Lee, Bruce Demple

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

In Escherichia coli, the SoxR regulon orchestrates genes for defense against certain types of oxidative stress through the SoxR-regulated synthesis of the SoxS transcription activator. The Pseudomonas putida genome did not reveal a clear soxS homolog. The P. putida SoxR protein appears to be functional: its expression in an E. coli ΔsoxR strain restored the paraquat inducibility of soxS. Of nine candidate P. putida oxidative stress genes, which are known to be SoxR regulon in E. coli, tested for response to superoxide or nitric oxide, fumC-1, sodA, zwf-1, and particularly fpr, encoding ferredoxin:NADP+ reductase, were induced, all independent of P. putida soxR. Disruption of the fpr and finR, a regulatory protein that is required for paraquat-dependent expression of the fpr, resulted in more oxidative stress sensitivity. However, a P. putida soxR-deletion strain had normal resistance to the superoxide-generating agent paraquat. The data presented here show that the genetic responses to superoxide stress in P. putida differ markedly from those seen in E. coli and Salmonella, and the role of P. putida soxR remains to be established.

Original languageEnglish
Pages (from-to)51-56
Number of pages6
JournalBiochemical and biophysical research communications
Volume341
Issue number1
DOIs
Publication statusPublished - 2006 Mar 3

Keywords

  • Biodegradation
  • Ferredoxin reductase
  • LysR-type transcriptional factor
  • Nitric oxide
  • Oxidative stress
  • Paraquat

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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