GlutaredoxinV1, Main, Exploration, bibRecord, 000141

OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli.

Identifieur interne : 000141 ( Main/Exploration ); précédent : 000140; suivant : 000142

OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli.

Auteurs : Ningke Hou [République populaire de Chine] ; Zhenzhen Yan [République populaire de Chine] ; Kaili Fan [République populaire de Chine] ; Huanjie Li [République populaire de Chine] ; Rui Zhao [République populaire de Chine] ; Yongzhen Xia [République populaire de Chine] ; Luying Xun [États-Unis] ; Huaiwei Liu [République populaire de Chine]

Source :

Redox biology [ 2213-2317 ] ; 2019.

RBID : pubmed:31421411

Descripteurs français

KwdFr :
- Activation de la transcription (MeSH), Analyse de profil d'expression de gènes (MeSH), Chromatographie en phase liquide (MeSH), Escherichia coli (physiologie), Mutation (MeSH), Oxydoréduction (MeSH), Peroxyde d'hydrogène (métabolisme), Protéines Escherichia coli (composition chimique), Protéines Escherichia coli (génétique), Protéines Escherichia coli (métabolisme), Protéines de répression (composition chimique), Protéines de répression (génétique), Protéines de répression (métabolisme), Régulation de l'expression des gènes bactériens (effets des médicaments et des substances chimiques), Soufre (métabolisme), Soufre (pharmacologie), Spectrométrie de masse en tandem (MeSH), Sulfure d'hydrogène (métabolisme), Thiorédoxines (métabolisme).
MESH :
- composition chimique : Protéines Escherichia coli, Protéines de répression.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes bactériens.
- génétique : Protéines Escherichia coli, Protéines de répression.
- métabolisme : Peroxyde d'hydrogène, Protéines Escherichia coli, Protéines de répression, Soufre, Sulfure d'hydrogène, Thiorédoxines.
- pharmacologie : Soufre.
- physiologie : Escherichia coli.
- Activation de la transcription, Analyse de profil d'expression de gènes, Chromatographie en phase liquide, Mutation, Oxydoréduction, Spectrométrie de masse en tandem.

English descriptors

KwdEn :
- Chromatography, Liquid (MeSH), Escherichia coli (physiology), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (genetics), Escherichia coli Proteins (metabolism), Gene Expression Profiling (MeSH), Gene Expression Regulation, Bacterial (drug effects), Hydrogen Peroxide (metabolism), Hydrogen Sulfide (metabolism), Mutation (MeSH), Oxidation-Reduction (MeSH), Repressor Proteins (chemistry), Repressor Proteins (genetics), Repressor Proteins (metabolism), Sulfur (metabolism), Sulfur (pharmacology), Tandem Mass Spectrometry (MeSH), Thioredoxins (metabolism), Transcriptional Activation (MeSH).
MESH :
- chemical , chemistry : Escherichia coli Proteins, Repressor Proteins.
- chemical , genetics : Escherichia coli Proteins, Repressor Proteins.
- chemical , metabolism : Escherichia coli Proteins, Hydrogen Peroxide, Hydrogen Sulfide, Repressor Proteins, Sulfur, Thioredoxins.
- drug effects : Gene Expression Regulation, Bacterial.
- chemical , pharmacology : Sulfur.
- physiology : Escherichia coli.
- Chromatography, Liquid, Gene Expression Profiling, Mutation, Oxidation-Reduction, Tandem Mass Spectrometry, Transcriptional Activation.

Abstract

Sulfane sulfur species including hydrogen polysulfide and organic persulfide are newly recognized normal cellular components, and they participate in signaling and protect cells from oxidative stress. Their production has been extensively studied, but their removal is less characterized. Herein, we showed that sulfane sulfur at high levels was toxic to Escherichia coli under both anaerobic and aerobic conditions. OxyR, a well-known regulator against H₂O₂, also sensed sulfane sulfur, as revealed via mutational analysis, constructed gene circuits, and in vitro gene expression. Hydrogen polysulfide modified OxyR at Cys199 to form a persulfide OxyR C199-SSH, and the modified OxyR activated the expression of thioredoxin 2 and glutaredoxin 1. The two enzymes are known to reduce sulfane sulfur to hydrogen sulfide. Bioinformatics analysis indicated that OxyR homologs are widely present in bacteria, including obligate anaerobic bacteria. Thus, the OxyR sensing of sulfane sulfur may represent a preserved mechanism for bacteria to deal with sulfane sulfur stress.

DOI: 10.1016/j.redox.2019.101293
PubMed: 31421411
PubMed Central: PMC6831875

Affiliations:

République populaire de Chine, États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000119
to stream Main, to step Curation: 000119

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Liquid (MeSH)</term>
<term>Escherichia coli (physiology)</term>
<term>Escherichia coli Proteins (chemistry)</term>
<term>Escherichia coli Proteins (genetics)</term>
<term>Escherichia coli Proteins (metabolism)</term>
<term>Gene Expression Profiling (MeSH)</term>
<term>Gene Expression Regulation, Bacterial (drug effects)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Hydrogen Sulfide (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Repressor Proteins (chemistry)</term>
<term>Repressor Proteins (genetics)</term>
<term>Repressor Proteins (metabolism)</term>
<term>Sulfur (metabolism)</term>
<term>Sulfur (pharmacology)</term>
<term>Tandem Mass Spectrometry (MeSH)</term>
<term>Thioredoxins (metabolism)</term>
<term>Transcriptional Activation (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation de la transcription (MeSH)</term>
<term>Analyse de profil d'expression de gènes (MeSH)</term>
<term>Chromatographie en phase liquide (MeSH)</term>
<term>Escherichia coli (physiologie)</term>
<term>Mutation (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxyde d'hydrogène (métabolisme)</term>
<term>Protéines Escherichia coli (composition chimique)</term>
<term>Protéines Escherichia coli (génétique)</term>
<term>Protéines Escherichia coli (métabolisme)</term>
<term>Protéines de répression (composition chimique)</term>
<term>Protéines de répression (génétique)</term>
<term>Protéines de répression (métabolisme)</term>
<term>Régulation de l'expression des gènes bactériens (effets des médicaments et des substances chimiques)</term>
<term>Soufre (métabolisme)</term>
<term>Soufre (pharmacologie)</term>
<term>Spectrométrie de masse en tandem (MeSH)</term>
<term>Sulfure d'hydrogène (métabolisme)</term>
<term>Thiorédoxines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Repressor Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Repressor Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Escherichia coli Proteins</term>
<term>Hydrogen Peroxide</term>
<term>Hydrogen Sulfide</term>
<term>Repressor Proteins</term>
<term>Sulfur</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines Escherichia coli</term>
<term>Protéines de répression</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Expression Regulation, Bacterial</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Régulation de l'expression des gènes bactériens</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines Escherichia coli</term>
<term>Protéines de répression</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peroxyde d'hydrogène</term>
<term>Protéines Escherichia coli</term>
<term>Protéines de répression</term>
<term>Soufre</term>
<term>Sulfure d'hydrogène</term>
<term>Thiorédoxines</term>
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<term>Mutation</term>
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<term>Tandem Mass Spectrometry</term>
<term>Transcriptional Activation</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Activation de la transcription</term>
<term>Analyse de profil d'expression de gènes</term>
<term>Chromatographie en phase liquide</term>
<term>Mutation</term>
<term>Oxydoréduction</term>
<term>Spectrométrie de masse en tandem</term>
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<front><div type="abstract" xml:lang="en">Sulfane sulfur species including hydrogen polysulfide and organic persulfide are newly recognized normal cellular components, and they participate in signaling and protect cells from oxidative stress. Their production has been extensively studied, but their removal is less characterized. Herein, we showed that sulfane sulfur at high levels was toxic to Escherichia coli under both anaerobic and aerobic conditions. OxyR, a well-known regulator against H<sub>2</sub>
O<sub>2</sub>
, also sensed sulfane sulfur, as revealed via mutational analysis, constructed gene circuits, and in vitro gene expression. Hydrogen polysulfide modified OxyR at Cys199 to form a persulfide OxyR C199-SSH, and the modified OxyR activated the expression of thioredoxin 2 and glutaredoxin 1. The two enzymes are known to reduce sulfane sulfur to hydrogen sulfide. Bioinformatics analysis indicated that OxyR homologs are widely present in bacteria, including obligate anaerobic bacteria. Thus, the OxyR sensing of sulfane sulfur may represent a preserved mechanism for bacteria to deal with sulfane sulfur stress.</div>
</front>
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<DateCompleted><Year>2020</Year>
<Month>02</Month>
<Day>27</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>02</Month>
<Day>27</Day>
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<JournalIssue CitedMedium="Internet"><Volume>26</Volume>
<PubDate><Year>2019</Year>
<Month>09</Month>
</PubDate>
</JournalIssue>
<Title>Redox biology</Title>
<ISOAbbreviation>Redox Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli.</ArticleTitle>
<Pagination><MedlinePgn>101293</MedlinePgn>
</Pagination>
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<Abstract><AbstractText>Sulfane sulfur species including hydrogen polysulfide and organic persulfide are newly recognized normal cellular components, and they participate in signaling and protect cells from oxidative stress. Their production has been extensively studied, but their removal is less characterized. Herein, we showed that sulfane sulfur at high levels was toxic to Escherichia coli under both anaerobic and aerobic conditions. OxyR, a well-known regulator against H<sub>2</sub>
O<sub>2</sub>
, also sensed sulfane sulfur, as revealed via mutational analysis, constructed gene circuits, and in vitro gene expression. Hydrogen polysulfide modified OxyR at Cys199 to form a persulfide OxyR C199-SSH, and the modified OxyR activated the expression of thioredoxin 2 and glutaredoxin 1. The two enzymes are known to reduce sulfane sulfur to hydrogen sulfide. Bioinformatics analysis indicated that OxyR homologs are widely present in bacteria, including obligate anaerobic bacteria. Thus, the OxyR sensing of sulfane sulfur may represent a preserved mechanism for bacteria to deal with sulfane sulfur stress.</AbstractText>
<CopyrightInformation>Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hou</LastName>
<ForeName>Ningke</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yan</LastName>
<ForeName>Zhenzhen</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fan</LastName>
<ForeName>Kaili</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Huanjie</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhao</LastName>
<ForeName>Rui</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xia</LastName>
<ForeName>Yongzhen</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xun</LastName>
<ForeName>Luying</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China; School of Molecular Biosciences, Washington State University, Pullman, WA, 99164-7520, USA. Electronic address: luying_xun@vetmed.edu.edu.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Huaiwei</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China. Electronic address: liuhuaiwei@sdu.edu.cn.</Affiliation>
</AffiliationInfo>
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   |texte=   OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli.
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Serveur d'exploration sur la glutarédoxine

OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli.

OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli.

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