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

doi:10.1016/j.bbrc.2005.12.142

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

64 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 language	English
Pages (from-to)	51-56
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	341
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2005.12.142
Publication status	Published - 2006 Mar 3

Bibliographical note

Funding Information:
S.P.-L. was supported by a postdoctoral fellowship from the Valencian Government (Generalitat Valenciana) in Spain. This work was supported by NCI, National Institutes of Health Grant CA37831 to B.D. and a NCRC (National Core Research Center) Grant (R15-2003-002-01002-0), a grant (R0503441) from BioGreen21 program, Rural Development Administration, and Ministry of Education and Human Resource Development (Grant R0508751), Republic of Korea to W.P.

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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10.1016/j.bbrc.2005.12.142

Cite this

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

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.",

keywords = "Biodegradation, Ferredoxin reductase, LysR-type transcriptional factor, Nitric oxide, Oxidative stress, Paraquat",

author = "Woojun Park and Samuel Pe{\~n}a-Llopis and Yunho Lee and Bruce Demple",

note = "Funding Information: S.P.-L. was supported by a postdoctoral fellowship from the Valencian Government (Generalitat Valenciana) in Spain. This work was supported by NCI, National Institutes of Health Grant CA37831 to B.D. and a NCRC (National Core Research Center) Grant (R15-2003-002-01002-0), a grant (R0503441) from BioGreen21 program, Rural Development Administration, and Ministry of Education and Human Resource Development (Grant R0508751), Republic of Korea to W.P.",

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AU - Park, Woojun

AU - Peña-Llopis, Samuel

AU - Lee, Yunho

AU - Demple, Bruce

N1 - Funding Information: S.P.-L. was supported by a postdoctoral fellowship from the Valencian Government (Generalitat Valenciana) in Spain. This work was supported by NCI, National Institutes of Health Grant CA37831 to B.D. and a NCRC (National Core Research Center) Grant (R15-2003-002-01002-0), a grant (R0503441) from BioGreen21 program, Rural Development Administration, and Ministry of Education and Human Resource Development (Grant R0508751), Republic of Korea to W.P.

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N2 - 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.

AB - 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.

KW - Biodegradation

KW - Ferredoxin reductase

KW - LysR-type transcriptional factor

KW - Nitric oxide

KW - Oxidative stress

KW - Paraquat

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SN - 0006-291X

VL - 341

SP - 51

EP - 56

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 1

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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