Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin.
Identifieur interne : 000888 ( Main/Exploration ); précédent : 000887; suivant : 000889Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin.
Auteurs : José F. Da Silva Neto [Brésil] ; Caroline C. Negretto ; Luis E S. NettoSource :
- PloS one [ 1932-6203 ] ; 2012.
Descripteurs français
- KwdFr :
- Chromobacterium (croissance et développement), Chromobacterium (effets des médicaments et des substances chimiques), Chromobacterium (génétique), Chromobacterium (métabolisme), Cystéine (MeSH), Disulfures (composition chimique), Mutation (MeSH), Oxydoréduction (MeSH), Peroxidases (génétique), Peroxidases (métabolisme), Peroxyde d'hydrogène (métabolisme), Peroxyde d'hydrogène (pharmacologie), Phylogenèse (MeSH), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Régions promotrices (génétique) (MeSH), Régulation de l'expression des gènes bactériens (effets des médicaments et des substances chimiques), Sites de fixation (MeSH), Séquence conservée (MeSH), Séquence nucléotidique (MeSH), Séquences répétées inversées (MeSH), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Disulfures.
- croissance et développement : Chromobacterium.
- effets des médicaments et des substances chimiques : Chromobacterium, Régulation de l'expression des gènes bactériens.
- génétique : Chromobacterium, Peroxidases, Protéines bactériennes, Thiorédoxines.
- métabolisme : Chromobacterium, Peroxidases, Peroxyde d'hydrogène, Protéines bactériennes, Thiorédoxines.
- pharmacologie : Peroxyde d'hydrogène.
- Cystéine, Mutation, Oxydoréduction, Phylogenèse, Régions promotrices (génétique), Sites de fixation, Séquence conservée, Séquence nucléotidique, Séquences répétées inversées.
English descriptors
- KwdEn :
- Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Base Sequence (MeSH), Binding Sites (MeSH), Chromobacterium (drug effects), Chromobacterium (genetics), Chromobacterium (growth & development), Chromobacterium (metabolism), Conserved Sequence (MeSH), Cysteine (MeSH), Disulfides (chemistry), Gene Expression Regulation, Bacterial (drug effects), Hydrogen Peroxide (metabolism), Hydrogen Peroxide (pharmacology), Inverted Repeat Sequences (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Peroxidases (genetics), Peroxidases (metabolism), Phylogeny (MeSH), Promoter Regions, Genetic (MeSH), Thioredoxins (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Disulfides.
- chemical , genetics : Bacterial Proteins, Peroxidases, Thioredoxins.
- chemical , metabolism : Bacterial Proteins, Hydrogen Peroxide, Peroxidases, Thioredoxins.
- drug effects : Chromobacterium, Gene Expression Regulation, Bacterial.
- genetics : Chromobacterium.
- growth & development : Chromobacterium.
- metabolism : Chromobacterium.
- chemical , pharmacology : Hydrogen Peroxide.
- Base Sequence, Binding Sites, Conserved Sequence, Cysteine, Inverted Repeat Sequences, Mutation, Oxidation-Reduction, Phylogeny, Promoter Regions, Genetic.
Abstract
Organic hydroperoxides are oxidants generated during bacterial-host interactions. Here, we demonstrate that the peroxidase OhrA and its negative regulator OhrR comprise a major pathway for sensing and detoxifying organic hydroperoxides in the opportunistic pathogen Chromobacterium violaceum. Initially, we found that an ohrA mutant was hypersensitive to organic hydroperoxides and that it displayed a low efficiency for decomposing these molecules. Expression of ohrA and ohrR was specifically induced by organic hydroperoxides. These genes were expressed as monocistronic transcripts and also as a bicistronic ohrR-ohrA mRNA, generating the abundantly detected ohrA mRNA and the barely detected ohrR transcript. The bicistronic transcript appears to be processed. OhrR repressed both the ohrA and ohrR genes by binding directly to inverted repeat sequences within their promoters in a redox-dependent manner. Site-directed mutagenesis of each of the four OhrR cysteine residues indicated that the conserved Cys21 is critical to organic hydroperoxide sensing, whereas Cys126 is required for disulfide bond formation. Taken together, these phenotypic, genetic and biochemical data indicate that the response of C. violaceum to organic hydroperoxides is mediated by OhrA and OhrR. Finally, we demonstrated that oxidized OhrR, inactivated by intermolecular disulfide bond formation, is specifically regenerated via thiol-disulfide exchange by thioredoxin (but not other thiol reducing agents such as glutaredoxin, glutathione and lipoamide), providing a physiological reducing system for this thiol-based redox switch.
DOI: 10.1371/journal.pone.0047090
PubMed: 23071722
PubMed Central: PMC3469484
Affiliations:
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inversées</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Organic hydroperoxides are oxidants generated during bacterial-host interactions. Here, we demonstrate that the peroxidase OhrA and its negative regulator OhrR comprise a major pathway for sensing and detoxifying organic hydroperoxides in the opportunistic pathogen Chromobacterium violaceum. Initially, we found that an ohrA mutant was hypersensitive to organic hydroperoxides and that it displayed a low efficiency for decomposing these molecules. Expression of ohrA and ohrR was specifically induced by organic hydroperoxides. These genes were expressed as monocistronic transcripts and also as a bicistronic ohrR-ohrA mRNA, generating the abundantly detected ohrA mRNA and the barely detected ohrR transcript. The bicistronic transcript appears to be processed. OhrR repressed both the ohrA and ohrR genes by binding directly to inverted repeat sequences within their promoters in a redox-dependent manner. Site-directed mutagenesis of each of the four OhrR cysteine residues indicated that the conserved Cys21 is critical to organic hydroperoxide sensing, whereas Cys126 is required for disulfide bond formation. Taken together, these phenotypic, genetic and biochemical data indicate that the response of C. violaceum to organic hydroperoxides is mediated by OhrA and OhrR. Finally, we demonstrated that oxidized OhrR, inactivated by intermolecular disulfide bond formation, is specifically regenerated via thiol-disulfide exchange by thioredoxin (but not other thiol reducing agents such as glutaredoxin, glutathione and lipoamide), providing a physiological reducing system for this thiol-based redox switch.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23071722</PMID><DateCompleted><Year>2013</Year><Month>05</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>10</Issue><PubDate><Year>2012</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin.</ArticleTitle><Pagination><MedlinePgn>e47090</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0047090</ELocationID><Abstract><AbstractText>Organic hydroperoxides are oxidants generated during bacterial-host interactions. Here, we demonstrate that the peroxidase OhrA and its negative regulator OhrR comprise a major pathway for sensing and detoxifying organic hydroperoxides in the opportunistic pathogen Chromobacterium violaceum. Initially, we found that an ohrA mutant was hypersensitive to organic hydroperoxides and that it displayed a low efficiency for decomposing these molecules. Expression of ohrA and ohrR was specifically induced by organic hydroperoxides. These genes were expressed as monocistronic transcripts and also as a bicistronic ohrR-ohrA mRNA, generating the abundantly detected ohrA mRNA and the barely detected ohrR transcript. The bicistronic transcript appears to be processed. OhrR repressed both the ohrA and ohrR genes by binding directly to inverted repeat sequences within their promoters in a redox-dependent manner. Site-directed mutagenesis of each of the four OhrR cysteine residues indicated that the conserved Cys21 is critical to organic hydroperoxide sensing, whereas Cys126 is required for disulfide bond formation. Taken together, these phenotypic, genetic and biochemical data indicate that the response of C. violaceum to organic hydroperoxides is mediated by OhrA and OhrR. Finally, we demonstrated that oxidized OhrR, inactivated by intermolecular disulfide bond formation, is specifically regenerated via thiol-disulfide exchange by thioredoxin (but not other thiol reducing agents such as glutaredoxin, glutathione and lipoamide), providing a physiological reducing system for this thiol-based redox switch.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>da Silva Neto</LastName><ForeName>José F</ForeName><Initials>JF</Initials><AffiliationInfo><Affiliation>Departamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Negretto</LastName><ForeName>Caroline C</ForeName><Initials>CC</Initials></Author><Author ValidYN="Y"><LastName>Netto</LastName><ForeName>Luis E S</ForeName><Initials>LE</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>10</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance 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development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015964" MajorTopicYN="N">Gene Expression Regulation, Bacterial</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055029" MajorTopicYN="N">Inverted Repeat Sequences</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011401" MajorTopicYN="N">Promoter Regions, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" 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Negretto</name><name sortKey="Netto, Luis E S" sort="Netto, Luis E S" uniqKey="Netto L" first="Luis E S" last="Netto">Luis E S. Netto</name></noCountry><country name="Brésil"><region name="État de São Paulo"><name sortKey="Da Silva Neto, Jose F" sort="Da Silva Neto, Jose F" uniqKey="Da Silva Neto J" first="José F" last="Da Silva Neto">José F. Da Silva Neto</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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