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Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti

BACKGROUND: Sinorhizobium meliloti is a symbiotic nitrogen-fixing bacterium that elicits nodules on roots of host plants Medicago sativa. During nodule formation bacteria have to withstand oxygen radicals produced by the plant. Resistance to H(2)O(2 )and superoxides has been extensively studied in S...

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Detalles Bibliográficos
Autores principales: Fontenelle, Catherine, Blanco, Carlos, Arrieta, Morgane, Dufour, Virginie, Trautwetter, Annie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3107159/
https://www.ncbi.nlm.nih.gov/pubmed/21569462
http://dx.doi.org/10.1186/1471-2180-11-100
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author Fontenelle, Catherine
Blanco, Carlos
Arrieta, Morgane
Dufour, Virginie
Trautwetter, Annie
author_facet Fontenelle, Catherine
Blanco, Carlos
Arrieta, Morgane
Dufour, Virginie
Trautwetter, Annie
author_sort Fontenelle, Catherine
collection PubMed
description BACKGROUND: Sinorhizobium meliloti is a symbiotic nitrogen-fixing bacterium that elicits nodules on roots of host plants Medicago sativa. During nodule formation bacteria have to withstand oxygen radicals produced by the plant. Resistance to H(2)O(2 )and superoxides has been extensively studied in S. meliloti. In contrast resistance to organic peroxides has not been investigated while S. meliloti genome encodes putative organic peroxidases. Organic peroxides are produced by plants and are highly toxic. The resistance to these oxygen radicals has been studied in various bacteria but never in plant nodulating bacteria. RESULTS: In this study we report the characterisation of organic hydroperoxide resistance gene ohr and its regulator ohrR in S. meliloti. The inactivation of ohr affects resistance to cumene and ter-butyl hydroperoxides but not to hydrogen peroxide or menadione in vitro. The expression of ohr and ohrR genes is specifically induced by organic peroxides. OhrR binds to the intergenic region between the divergent genes ohr and ohrR. Two binding sites were characterised. Binding to the operator is prevented by OhrR oxidation that promotes OhrR dimerisation. The inactivation of ohr did not affect symbiosis and nitrogen fixation, suggesting that redundant enzymatic activity exists in this strain. Both ohr and ohrR are expressed in nodules suggesting that they play a role during nitrogen fixation. CONCLUSIONS: This report demonstrates the significant role Ohr and OhrR proteins play in bacterial stress resistance against organic peroxides in S. meliloti. The ohr and ohrR genes are expressed in nodule-inhabiting bacteroids suggesting a role during nodulation.
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spelling pubmed-31071592011-06-03 Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti Fontenelle, Catherine Blanco, Carlos Arrieta, Morgane Dufour, Virginie Trautwetter, Annie BMC Microbiol Research Article BACKGROUND: Sinorhizobium meliloti is a symbiotic nitrogen-fixing bacterium that elicits nodules on roots of host plants Medicago sativa. During nodule formation bacteria have to withstand oxygen radicals produced by the plant. Resistance to H(2)O(2 )and superoxides has been extensively studied in S. meliloti. In contrast resistance to organic peroxides has not been investigated while S. meliloti genome encodes putative organic peroxidases. Organic peroxides are produced by plants and are highly toxic. The resistance to these oxygen radicals has been studied in various bacteria but never in plant nodulating bacteria. RESULTS: In this study we report the characterisation of organic hydroperoxide resistance gene ohr and its regulator ohrR in S. meliloti. The inactivation of ohr affects resistance to cumene and ter-butyl hydroperoxides but not to hydrogen peroxide or menadione in vitro. The expression of ohr and ohrR genes is specifically induced by organic peroxides. OhrR binds to the intergenic region between the divergent genes ohr and ohrR. Two binding sites were characterised. Binding to the operator is prevented by OhrR oxidation that promotes OhrR dimerisation. The inactivation of ohr did not affect symbiosis and nitrogen fixation, suggesting that redundant enzymatic activity exists in this strain. Both ohr and ohrR are expressed in nodules suggesting that they play a role during nitrogen fixation. CONCLUSIONS: This report demonstrates the significant role Ohr and OhrR proteins play in bacterial stress resistance against organic peroxides in S. meliloti. The ohr and ohrR genes are expressed in nodule-inhabiting bacteroids suggesting a role during nodulation. BioMed Central 2011-05-13 /pmc/articles/PMC3107159/ /pubmed/21569462 http://dx.doi.org/10.1186/1471-2180-11-100 Text en Copyright ©2011 Fontenelle et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Fontenelle, Catherine
Blanco, Carlos
Arrieta, Morgane
Dufour, Virginie
Trautwetter, Annie
Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti
title Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti
title_full Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti
title_fullStr Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti
title_full_unstemmed Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti
title_short Resistance to organic hydroperoxides requires ohr and ohrR genes in Sinorhizobium meliloti
title_sort resistance to organic hydroperoxides requires ohr and ohrr genes in sinorhizobium meliloti
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3107159/
https://www.ncbi.nlm.nih.gov/pubmed/21569462
http://dx.doi.org/10.1186/1471-2180-11-100
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