Glutaredoxin s12: unique properties for redox signaling.
Identifieur interne : 002A50 ( Main/Exploration ); précédent : 002A49; suivant : 002A51Glutaredoxin s12: unique properties for redox signaling.
Auteurs : Mirko Zaffagnini [France] ; Mariette Bedhomme ; Christophe H. Marchand ; J R My Couturier ; Xing-Huang Gao ; Nicolas Rouhier ; Paolo Trost ; St Phane D. LemaireSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2012.
Descripteurs français
- KwdFr :
- 2-Iodo-acétamide (pharmacologie), Activation enzymatique (effets des médicaments et des substances chimiques), Alkylation (MeSH), Antienzymes (pharmacologie), Catalyse (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Domaine catalytique (MeSH), Glutarédoxines (antagonistes et inhibiteurs), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Oxydoréduction (MeSH), Populus (enzymologie), Spécificité du substrat (MeSH), Substitution d'acide aminé (MeSH), Transduction du signal (MeSH).
- MESH :
- antagonistes et inhibiteurs : Glutarédoxines.
- effets des médicaments et des substances chimiques : Activation enzymatique.
- enzymologie : Populus.
- génétique : Glutarédoxines.
- métabolisme : Glutarédoxines.
- pharmacologie : 2-Iodo-acétamide, Antienzymes.
- Alkylation, Catalyse, Cinétique, Concentration en ions d'hydrogène, Domaine catalytique, Oxydoréduction, Spécificité du substrat, Substitution d'acide aminé, Transduction du signal.
English descriptors
- KwdEn :
- Alkylation (MeSH), Amino Acid Substitution (MeSH), Catalysis (MeSH), Catalytic Domain (MeSH), Enzyme Activation (drug effects), Enzyme Inhibitors (pharmacology), Glutaredoxins (antagonists & inhibitors), Glutaredoxins (genetics), Glutaredoxins (metabolism), Hydrogen-Ion Concentration (MeSH), Iodoacetamide (pharmacology), Kinetics (MeSH), Oxidation-Reduction (MeSH), Populus (enzymology), Signal Transduction (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Glutaredoxins.
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Glutaredoxins.
- chemical , pharmacology : Enzyme Inhibitors, Iodoacetamide.
- drug effects : Enzyme Activation.
- enzymology : Populus.
- Alkylation, Amino Acid Substitution, Catalysis, Catalytic Domain, Hydrogen-Ion Concentration, Kinetics, Oxidation-Reduction, Signal Transduction, Substrate Specificity.
Abstract
AIMS
Cysteines (Cys) made acidic by the protein environment are generally sensitive to pro-oxidant molecules. Glutathionylation is a post-translational modification that can occur by spontaneous reaction of reduced glutathione (GSH) with oxidized Cys as sulfenic acids (-SOH). The reverse reaction (deglutathionylation) is strongly stimulated by glutaredoxins (Grx) and requires a reductant, often GSH.
RESULTS
Here, we show that chloroplast GrxS12 from poplar efficiently reacts with glutathionylated substrates in a GSH-dependent ping pong mechanism. The pK(a) of GrxS12 catalytic Cys is very low (3.9) and makes GrxS12 itself sensitive to oxidation by H(2)O(2) and to direct glutathionylation by nitrosoglutathione. Glutathionylated-GrxS12 (GrxS12-SSG) is temporarily inactive until it is deglutathionylated by GSH. The equilibrium between GrxS12 and glutathione (E(m(GrxS12-SSG))= -315 mV, pH 7.0) is characterized by K(ox) values of 310 at pH 7.0, as in darkened chloroplasts, and 69 at pH 7.9, as in illuminated chloroplasts.
INNOVATION
Based on thermodynamic data, GrxS12-SSG is predicted to accumulate in vivo under conditions of mild oxidation of the GSH pool that may occur under stress. Moreover, GrxS12-SSG is predicted to be more stable in chloroplasts in the dark than in the light.
CONCLUSION
These peculiar catalytic and thermodynamic properties could allow GrxS12 to act as a stress-related redox sensor, thus allowing glutathione to play a signaling role through glutathionylation of GrxS12 target proteins.
DOI: 10.1089/ars.2011.3933
PubMed: 21707412
Affiliations:
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Marchand</name></author><author><name sortKey="Couturier, J R My" sort="Couturier, J R My" uniqKey="Couturier J" first="J R My" last="Couturier">J R My Couturier</name></author><author><name sortKey="Gao, Xing Huang" sort="Gao, Xing Huang" uniqKey="Gao X" first="Xing-Huang" last="Gao">Xing-Huang Gao</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author><author><name sortKey="Trost, Paolo" sort="Trost, Paolo" uniqKey="Trost P" first="Paolo" last="Trost">Paolo Trost</name></author><author><name sortKey="Lemaire, St Phane D" sort="Lemaire, St Phane D" uniqKey="Lemaire S" first="St Phane D" last="Lemaire">St Phane D. 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Marchand</name></author><author><name sortKey="Couturier, J R My" sort="Couturier, J R My" uniqKey="Couturier J" first="J R My" last="Couturier">J R My Couturier</name></author><author><name sortKey="Gao, Xing Huang" sort="Gao, Xing Huang" uniqKey="Gao X" first="Xing-Huang" last="Gao">Xing-Huang Gao</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author><author><name sortKey="Trost, Paolo" sort="Trost, Paolo" uniqKey="Trost P" first="Paolo" last="Trost">Paolo Trost</name></author><author><name sortKey="Lemaire, St Phane D" sort="Lemaire, St Phane D" uniqKey="Lemaire S" first="St Phane D" last="Lemaire">St Phane D. Lemaire</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alkylation (MeSH)</term><term>Amino Acid Substitution (MeSH)</term><term>Catalysis (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Enzyme Activation (drug effects)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Glutaredoxins (antagonists & inhibitors)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Iodoacetamide (pharmacology)</term><term>Kinetics (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Populus (enzymology)</term><term>Signal Transduction (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>2-Iodo-acétamide (pharmacologie)</term><term>Activation enzymatique (effets des médicaments et des substances chimiques)</term><term>Alkylation (MeSH)</term><term>Antienzymes (pharmacologie)</term><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Glutarédoxines (antagonistes et inhibiteurs)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Populus (enzymologie)</term><term>Spécificité du substrat (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Iodoacetamide</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Activation</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Activation enzymatique</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>2-Iodo-acétamide</term><term>Antienzymes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Alkylation</term><term>Amino Acid Substitution</term><term>Catalysis</term><term>Catalytic Domain</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Oxidation-Reduction</term><term>Signal Transduction</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alkylation</term><term>Catalyse</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Domaine catalytique</term><term>Oxydoréduction</term><term>Spécificité du substrat</term><term>Substitution d'acide aminé</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Cysteines (Cys) made acidic by the protein environment are generally sensitive to pro-oxidant molecules. Glutathionylation is a post-translational modification that can occur by spontaneous reaction of reduced glutathione (GSH) with oxidized Cys as sulfenic acids (-SOH). The reverse reaction (deglutathionylation) is strongly stimulated by glutaredoxins (Grx) and requires a reductant, often GSH.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Here, we show that chloroplast GrxS12 from poplar efficiently reacts with glutathionylated substrates in a GSH-dependent ping pong mechanism. The pK(a) of GrxS12 catalytic Cys is very low (3.9) and makes GrxS12 itself sensitive to oxidation by H(2)O(2) and to direct glutathionylation by nitrosoglutathione. Glutathionylated-GrxS12 (GrxS12-SSG) is temporarily inactive until it is deglutathionylated by GSH. The equilibrium between GrxS12 and glutathione (E(m(GrxS12-SSG))= -315 mV, pH 7.0) is characterized by K(ox) values of 310 at pH 7.0, as in darkened chloroplasts, and 69 at pH 7.9, as in illuminated chloroplasts.</p></div><div type="abstract" xml:lang="en"><p><b>INNOVATION</b></p><p>Based on thermodynamic data, GrxS12-SSG is predicted to accumulate in vivo under conditions of mild oxidation of the GSH pool that may occur under stress. Moreover, GrxS12-SSG is predicted to be more stable in chloroplasts in the dark than in the light.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>These peculiar catalytic and thermodynamic properties could allow GrxS12 to act as a stress-related redox sensor, thus allowing glutathione to play a signaling role through glutathionylation of GrxS12 target proteins.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21707412</PMID><DateCompleted><Year>2012</Year><Month>03</Month><Day>09</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Jan</Month><Day>01</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxin s12: unique properties for redox signaling.</ArticleTitle><Pagination><MedlinePgn>17-32</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2011.3933</ELocationID><Abstract><AbstractText Label="AIMS" NlmCategory="OBJECTIVE">Cysteines (Cys) made acidic by the protein environment are generally sensitive to pro-oxidant molecules. Glutathionylation is a post-translational modification that can occur by spontaneous reaction of reduced glutathione (GSH) with oxidized Cys as sulfenic acids (-SOH). The reverse reaction (deglutathionylation) is strongly stimulated by glutaredoxins (Grx) and requires a reductant, often GSH.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Here, we show that chloroplast GrxS12 from poplar efficiently reacts with glutathionylated substrates in a GSH-dependent ping pong mechanism. The pK(a) of GrxS12 catalytic Cys is very low (3.9) and makes GrxS12 itself sensitive to oxidation by H(2)O(2) and to direct glutathionylation by nitrosoglutathione. Glutathionylated-GrxS12 (GrxS12-SSG) is temporarily inactive until it is deglutathionylated by GSH. The equilibrium between GrxS12 and glutathione (E(m(GrxS12-SSG))= -315 mV, pH 7.0) is characterized by K(ox) values of 310 at pH 7.0, as in darkened chloroplasts, and 69 at pH 7.9, as in illuminated chloroplasts.</AbstractText><AbstractText Label="INNOVATION" NlmCategory="METHODS">Based on thermodynamic data, GrxS12-SSG is predicted to accumulate in vivo under conditions of mild oxidation of the GSH pool that may occur under stress. Moreover, GrxS12-SSG is predicted to be more stable in chloroplasts in the dark than in the light.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">These peculiar catalytic and thermodynamic properties could allow GrxS12 to act as a stress-related redox sensor, thus allowing glutathione to play a signaling role through glutathionylation of GrxS12 target proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zaffagnini</LastName><ForeName>Mirko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, FRE3354 Centre National de la Recherche Scientifique, Institut de Biologie Physico-Chimique, Université Pierre et Marie Curies, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bedhomme</LastName><ForeName>Mariette</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Marchand</LastName><ForeName>Christophe H</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>J R My</ForeName><Initials>JR</Initials></Author><Author ValidYN="Y"><LastName>Gao</LastName><ForeName>Xing-Huang</ForeName><Initials>XH</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Trost</LastName><ForeName>Paolo</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Lemaire</LastName><ForeName>St Phane D</ForeName><Initials>SP</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>2011</Year><Month>08</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>ZRH8M27S79</RegistryNumber><NameOfSubstance UI="D007460">Iodoacetamide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000478" MajorTopicYN="N">Alkylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007460" MajorTopicYN="N">Iodoacetamide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>6</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>6</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21707412</ArticleId><ArticleId IdType="doi">10.1089/ars.2011.3933</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><noCountry><name sortKey="Bedhomme, Mariette" sort="Bedhomme, Mariette" uniqKey="Bedhomme M" first="Mariette" last="Bedhomme">Mariette Bedhomme</name><name sortKey="Couturier, J R My" sort="Couturier, J R My" uniqKey="Couturier J" first="J R My" last="Couturier">J R My Couturier</name><name sortKey="Gao, Xing Huang" sort="Gao, Xing Huang" uniqKey="Gao X" first="Xing-Huang" last="Gao">Xing-Huang Gao</name><name sortKey="Lemaire, St Phane D" sort="Lemaire, St Phane D" uniqKey="Lemaire S" first="St Phane D" last="Lemaire">St Phane D. Lemaire</name><name sortKey="Marchand, Christophe H" sort="Marchand, Christophe H" uniqKey="Marchand C" first="Christophe H" last="Marchand">Christophe H. Marchand</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Trost, Paolo" sort="Trost, Paolo" uniqKey="Trost P" first="Paolo" last="Trost">Paolo Trost</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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