The thioredoxin-mediated recycling of Arabidopsis thaliana GRXS16 relies on a conserved C-terminal cysteine.
Identifieur interne : 000107 ( Main/Exploration ); précédent : 000106; suivant : 000108The thioredoxin-mediated recycling of Arabidopsis thaliana GRXS16 relies on a conserved C-terminal cysteine.
Auteurs : Flavien Zannini [France] ; Anna Moseler [Allemagne] ; Raphaël Bchini [France] ; Tiphaine Dhalleine [France] ; Andreas J. Meyer [Allemagne] ; Nicolas Rouhier [France] ; Jérémy Couturier [France]Source :
- Biochimica et biophysica acta. General subjects [ 1872-8006 ] ; 2019.
Descripteurs français
- KwdFr :
- Alkylation (MeSH), Arabidopsis (métabolisme), Cystéine (métabolisme), Endonucleases (analyse), Endonucleases (génétique), Endonucleases (métabolisme), Oxydoréduction (MeSH), Protéines d'Arabidopsis (analyse), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Spectrométrie de masse (MeSH), Thiorédoxines (métabolisme).
- MESH :
- analyse : Endonucleases, Protéines d'Arabidopsis.
- génétique : Endonucleases, Protéines d'Arabidopsis.
- métabolisme : Arabidopsis, Cystéine, Endonucleases, Protéines d'Arabidopsis, Thiorédoxines.
- Alkylation, Oxydoréduction, Spectrométrie de masse.
English descriptors
- KwdEn :
- Alkylation (MeSH), Arabidopsis (metabolism), Arabidopsis Proteins (analysis), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Cysteine (metabolism), Endonucleases (analysis), Endonucleases (genetics), Endonucleases (metabolism), Mass Spectrometry (MeSH), Oxidation-Reduction (MeSH), Thioredoxins (metabolism).
- MESH :
- chemical , analysis : Arabidopsis Proteins, Endonucleases.
- chemical , genetics : Arabidopsis Proteins, Endonucleases.
- metabolism : Arabidopsis, Arabidopsis Proteins, Cysteine, Endonucleases, Thioredoxins.
- Alkylation, Mass Spectrometry, Oxidation-Reduction.
Abstract
BACKGROUND
Glutaredoxins (GRXs) are oxidoreductases involved in diverse cellular processes through their capacity to reduce glutathionylated proteins and/or to coordinate iron‑sulfur (Fe-S) clusters. Among class II GRXs, the plant-specific GRXS16 is a bimodular protein formed by an N-terminal endonuclease domain fused to a GRX domain containing a
METHODS
The biochemical properties (redox activity, sensitivity to oxidation, pK
RESULTS
Activity measurements using redox-sensitive GFP2 (roGFP2) as target protein did not reveal any significant glutathione-dependent reductase activity of A. thaliana GRXS16 whereas it was able to catalyze the oxidation of roGFP2 in the presence of glutathione disulfide. Accordingly, Arabidopsis GRXS16 reacted efficiently with oxidized forms of glutathione, leading to the formation of an intramolecular disulfide between Cys
CONCLUSION
The reduction of AtGRXS16, which is mandatory for its oxidoreductase activity and the binding of Fe-S clusters, depends on light through the plastidial FTR/TRX system. Hence, disulfide formation may constitute a redox switch mechanism controlling GRXS16 function in response to day/night transition or oxidizing conditions.
GENERAL SIGNIFICANCE
From the in vitro data obtained with roGFP2, one can postulate that GRXS16 would mediate protein glutathionylation/oxidation in plastids but not their deglutathionylation.
DOI: 10.1016/j.bbagen.2018.11.014
PubMed: 30502392
Affiliations:
- Allemagne, France
- District de Cologne, Grand Est, Lorraine (région), Rhénanie-du-Nord-Westphalie
- Bonn, Nancy
- Université de Lorraine
Links toward previous steps (curation, corpus...)
Le document en format XML
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Meyer</name><affiliation wicri:level="3"><nlm:affiliation>INRES-Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, 53113, Bonn, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>INRES-Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, 53113, Bonn</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Bonn</settlement></placeName></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.. Electronic address: jeremy.couturier@univ-lorraine.fr.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">France</country><wicri:regionArea>Université de Lorraine, Inra, IAM, F-54000 Nancy</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Nancy</settlement></placeName><orgName type="university">Université de Lorraine</orgName></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. General subjects</title><idno type="eISSN">1872-8006</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alkylation (MeSH)</term><term>Arabidopsis (metabolism)</term><term>Arabidopsis Proteins (analysis)</term><term>Arabidopsis Proteins (genetics)</term><term>Arabidopsis Proteins (metabolism)</term><term>Cysteine (metabolism)</term><term>Endonucleases (analysis)</term><term>Endonucleases (genetics)</term><term>Endonucleases (metabolism)</term><term>Mass Spectrometry (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alkylation (MeSH)</term><term>Arabidopsis (métabolisme)</term><term>Cystéine (métabolisme)</term><term>Endonucleases (analyse)</term><term>Endonucleases (génétique)</term><term>Endonucleases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Protéines d'Arabidopsis (analyse)</term><term>Protéines d'Arabidopsis (génétique)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Spectrométrie de masse (MeSH)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Arabidopsis Proteins</term><term>Endonucleases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabidopsis Proteins</term><term>Endonucleases</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Endonucleases</term><term>Protéines d'Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Endonucleases</term><term>Protéines d'Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term><term>Arabidopsis Proteins</term><term>Cysteine</term><term>Endonucleases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term><term>Cystéine</term><term>Endonucleases</term><term>Protéines d'Arabidopsis</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Alkylation</term><term>Mass Spectrometry</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alkylation</term><term>Oxydoréduction</term><term>Spectrométrie de masse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Glutaredoxins (GRXs) are oxidoreductases involved in diverse cellular processes through their capacity to reduce glutathionylated proteins and/or to coordinate iron‑sulfur (Fe-S) clusters. Among class II GRXs, the plant-specific GRXS16 is a bimodular protein formed by an N-terminal endonuclease domain fused to a GRX domain containing a </p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>The biochemical properties (redox activity, sensitivity to oxidation, pK</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Activity measurements using redox-sensitive GFP2 (roGFP2) as target protein did not reveal any significant glutathione-dependent reductase activity of A. thaliana GRXS16 whereas it was able to catalyze the oxidation of roGFP2 in the presence of glutathione disulfide. Accordingly, Arabidopsis GRXS16 reacted efficiently with oxidized forms of glutathione, leading to the formation of an intramolecular disulfide between Cys</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>The reduction of AtGRXS16, which is mandatory for its oxidoreductase activity and the binding of Fe-S clusters, depends on light through the plastidial FTR/TRX system. Hence, disulfide formation may constitute a redox switch mechanism controlling GRXS16 function in response to day/night transition or oxidizing conditions.</p></div><div type="abstract" xml:lang="en"><p><b>GENERAL SIGNIFICANCE</b></p><p>From the in vitro data obtained with roGFP2, one can postulate that GRXS16 would mediate protein glutathionylation/oxidation in plastids but not their deglutathionylation.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30502392</PMID><DateCompleted><Year>2019</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-8006</ISSN><JournalIssue CitedMedium="Internet"><Volume>1863</Volume><Issue>2</Issue><PubDate><Year>2019</Year><Month>02</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. General subjects</Title><ISOAbbreviation>Biochim Biophys Acta Gen Subj</ISOAbbreviation></Journal><ArticleTitle>The thioredoxin-mediated recycling of Arabidopsis thaliana GRXS16 relies on a conserved C-terminal cysteine.</ArticleTitle><Pagination><MedlinePgn>426-436</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(18)30363-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2018.11.014</ELocationID><Abstract><AbstractText Label="BACKGROUND">Glutaredoxins (GRXs) are oxidoreductases involved in diverse cellular processes through their capacity to reduce glutathionylated proteins and/or to coordinate iron‑sulfur (Fe-S) clusters. Among class II GRXs, the plant-specific GRXS16 is a bimodular protein formed by an N-terminal endonuclease domain fused to a GRX domain containing a <sup>158</sup>CGFS signature.</AbstractText><AbstractText Label="METHODS">The biochemical properties (redox activity, sensitivity to oxidation, pK<sub>a</sub> of cysteine residues, midpoint redox potential) of Arabidopsis thaliana GRXS16 were investigated by coupling oxidative treatments to alkylation shift assays, activity measurements and mass spectrometry analyses.</AbstractText><AbstractText Label="RESULTS">Activity measurements using redox-sensitive GFP2 (roGFP2) as target protein did not reveal any significant glutathione-dependent reductase activity of A. thaliana GRXS16 whereas it was able to catalyze the oxidation of roGFP2 in the presence of glutathione disulfide. Accordingly, Arabidopsis GRXS16 reacted efficiently with oxidized forms of glutathione, leading to the formation of an intramolecular disulfide between Cys<sup>158</sup> and the semi-conserved Cys<sup>215</sup>, which has a midpoint redox potential of - 298 mV at pH 7.0 and is reduced by plastidial thioredoxins (TRXs) but not GSH. By promoting the formation of this disulfide, Cys<sup>215</sup> modulates GRXS16 oxidoreductase activity.</AbstractText><AbstractText Label="CONCLUSION">The reduction of AtGRXS16, which is mandatory for its oxidoreductase activity and the binding of Fe-S clusters, depends on light through the plastidial FTR/TRX system. Hence, disulfide formation may constitute a redox switch mechanism controlling GRXS16 function in response to day/night transition or oxidizing conditions.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE">From the in vitro data obtained with roGFP2, one can postulate that GRXS16 would mediate protein glutathionylation/oxidation in plastids but not their deglutathionylation.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zannini</LastName><ForeName>Flavien</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moseler</LastName><ForeName>Anna</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.; INRES-Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, 53113, Bonn, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bchini</LastName><ForeName>Raphaël</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dhalleine</LastName><ForeName>Tiphaine</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meyer</LastName><ForeName>Andreas J</ForeName><Initials>AJ</Initials><AffiliationInfo><Affiliation>INRES-Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, 53113, Bonn, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Université de Lorraine, Inra, IAM, F-54000 Nancy, France.. Electronic address: jeremy.couturier@univ-lorraine.fr.</Affiliation></AffiliationInfo></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>2018</Year><Month>11</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Gen Subj</MedlineTA><NlmUniqueID>101731726</NlmUniqueID><ISSNLinking>0304-4165</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="D004720">Endonucleases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="C582684">GRXS16 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000478" MajorTopicYN="N">Alkylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004720" MajorTopicYN="N">Endonucleases</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Chloroplast</Keyword><Keyword MajorTopicYN="Y">Disulfide bond</Keyword><Keyword MajorTopicYN="Y">Glutaredoxin</Keyword><Keyword MajorTopicYN="Y">Redox regulation</Keyword><Keyword MajorTopicYN="Y">Thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>06</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>11</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>11</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>12</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>10</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>12</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30502392</ArticleId><ArticleId IdType="pii">S0304-4165(18)30363-5</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2018.11.014</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>France</li></country><region><li>District de Cologne</li><li>Grand Est</li><li>Lorraine (région)</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Bonn</li><li>Nancy</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><country name="France"><region name="Grand Est"><name sortKey="Zannini, Flavien" sort="Zannini, Flavien" uniqKey="Zannini F" first="Flavien" last="Zannini">Flavien Zannini</name></region><name sortKey="Bchini, Raphael" sort="Bchini, Raphael" uniqKey="Bchini R" first="Raphaël" last="Bchini">Raphaël Bchini</name><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><name sortKey="Dhalleine, Tiphaine" sort="Dhalleine, Tiphaine" uniqKey="Dhalleine T" first="Tiphaine" last="Dhalleine">Tiphaine Dhalleine</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></country><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Moseler, Anna" sort="Moseler, Anna" uniqKey="Moseler A" first="Anna" last="Moseler">Anna Moseler</name></region><name sortKey="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. 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