GlutaredoxinV1, Main, Exploration, bibRecord, 000271

Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.

Identifieur interne : 000271 ( Main/Exploration ); précédent : 000270; suivant : 000272

Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.

Auteurs : Maria-Armineh Tossounian [Belgique] ; Inge Van Molle [Belgique] ; Khadija Wahni [Belgique] ; Silke Jacques [Belgique] ; Kris Gevaert [Belgique] ; Frank Van Breusegem [Belgique] ; Didier Vertommen [Belgique] ; David Young [Belgique] ; Leonardo Astolfi Rosado [Belgique] ; Joris Messens [Belgique]

Source :

Biochimica et biophysica acta. General subjects [ 0304-4165 ] ; 2018.

RBID : pubmed:29031766

Descripteurs français

KwdFr :
- Agents protecteurs (métabolisme), Arabidopsis (croissance et développement), Arabidopsis (enzymologie), Catalyse (MeSH), Disulfure de glutathion (métabolisme), Disulfures (métabolisme), Glutarédoxines (métabolisme), Glutathione transferase (composition chimique), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Méthionine (analogues et dérivés), Méthionine (métabolisme), Peroxyde d'hydrogène (métabolisme), Stress oxydatif (MeSH).
MESH :
- analogues et dérivés : Méthionine.
- composition chimique : Glutathione transferase.
- croissance et développement : Arabidopsis.
- enzymologie : Arabidopsis.
- génétique : Glutathione transferase.
- métabolisme : Agents protecteurs, Disulfure de glutathion, Disulfures, Glutarédoxines, Glutathione transferase, Méthionine, Peroxyde d'hydrogène.
- Catalyse, Stress oxydatif.

English descriptors

KwdEn :
- Arabidopsis (enzymology), Arabidopsis (growth & development), Catalysis (MeSH), Disulfides (metabolism), Glutaredoxins (metabolism), Glutathione Disulfide (metabolism), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Hydrogen Peroxide (metabolism), Methionine (analogs & derivatives), Methionine (metabolism), Oxidative Stress (MeSH), Protective Agents (metabolism).
MESH :
- chemical , analogs & derivatives : Methionine.
- chemical , chemistry : Glutathione Transferase.
- chemical , genetics : Glutathione Transferase.
- chemical , metabolism : Disulfides, Glutaredoxins, Glutathione Disulfide, Glutathione Transferase, Hydrogen Peroxide, Methionine, Protective Agents.
- enzymology : Arabidopsis.
- growth & development : Arabidopsis.
- Catalysis, Oxidative Stress.

Abstract

BACKGROUND

Glutathione transferases play an important role as detoxifying enzymes. In A. thaliana, elevated levels of reactive oxygen species (ROS), provoked during biotic and abiotic stress, influence the activity of GSTU23. The aim of this study is to determine the impact of oxidative stress on the function and structure of GSTU23.

METHODS

The impact of oxidation on the function of GSTU23 was studied using a glutathione transferase biochemical assay and mass spectrometry. With kinetics, circular dichroism and thermodynamics, we compared reduced with oxidized GSTU23. X-ray crystal structures of GSTU23 visualize the impact of oxidation on methionines and cysteines.

RESULTS

In the presence of 100μM H

CONCLUSIONS AND SIGNIFICANCE

At lower H

DOI: 10.1016/j.bbagen.2017.10.007
PubMed: 29031766

Affiliations:

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

to stream Main, to step Corpus: 000302
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Le document en format XML

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<affiliation wicri:level="1"><nlm:affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.</nlm:affiliation>
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<author><name sortKey="Van Breusegem, Frank" sort="Van Breusegem, Frank" uniqKey="Van Breusegem F" first="Frank" last="Van Breusegem">Frank Van Breusegem</name>
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<author><name sortKey="Vertommen, Didier" sort="Vertommen, Didier" uniqKey="Vertommen D" first="Didier" last="Vertommen">Didier Vertommen</name>
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<country xml:lang="fr">Belgique</country>
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<term>Arabidopsis (growth & development)</term>
<term>Catalysis (MeSH)</term>
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<term>Methionine (metabolism)</term>
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<term>Peroxyde d'hydrogène (métabolisme)</term>
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<term>Glutathione transferase</term>
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</teiHeader>
<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>Glutathione transferases play an important role as detoxifying enzymes. In A. thaliana, elevated levels of reactive oxygen species (ROS), provoked during biotic and abiotic stress, influence the activity of GSTU23. The aim of this study is to determine the impact of oxidative stress on the function and structure of GSTU23.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>METHODS</b>
</p>
<p>The impact of oxidation on the function of GSTU23 was studied using a glutathione transferase biochemical assay and mass spectrometry. With kinetics, circular dichroism and thermodynamics, we compared reduced with oxidized GSTU23. X-ray crystal structures of GSTU23 visualize the impact of oxidation on methionines and cysteines.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>In the presence of 100μM H</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSIONS AND SIGNIFICANCE</b>
</p>
<p>At lower H</p>
</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29031766</PMID>
<DateCompleted><Year>2018</Year>
<Month>11</Month>
<Day>01</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>01</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0304-4165</ISSN>
<JournalIssue CitedMedium="Print"><Volume>1862</Volume>
<Issue>3</Issue>
<PubDate><Year>2018</Year>
<Month>03</Month>
</PubDate>
</JournalIssue>
<Title>Biochimica et biophysica acta. General subjects</Title>
<ISOAbbreviation>Biochim Biophys Acta Gen Subj</ISOAbbreviation>
</Journal>
<ArticleTitle>Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.</ArticleTitle>
<Pagination><MedlinePgn>775-789</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S0304-4165(17)30328-8</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2017.10.007</ELocationID>
<Abstract><AbstractText Label="BACKGROUND">Glutathione transferases play an important role as detoxifying enzymes. In A. thaliana, elevated levels of reactive oxygen species (ROS), provoked during biotic and abiotic stress, influence the activity of GSTU23. The aim of this study is to determine the impact of oxidative stress on the function and structure of GSTU23.</AbstractText>
<AbstractText Label="METHODS">The impact of oxidation on the function of GSTU23 was studied using a glutathione transferase biochemical assay and mass spectrometry. With kinetics, circular dichroism and thermodynamics, we compared reduced with oxidized GSTU23. X-ray crystal structures of GSTU23 visualize the impact of oxidation on methionines and cysteines.</AbstractText>
<AbstractText Label="RESULTS">In the presence of 100μM H<sub>2</sub>
O<sub>2</sub>
, oxidation of the methionine side-chain to a sulfoxide is the prominent post-translational modification, which can be reduced by C. diphtheriae MsrA and MsrB. However, increasing the level to 200μM H<sub>2</sub>
O<sub>2</sub>
 results in a reversible intramolecular disulfide between Cys65-Cys110, which is substrate for glutaredoxin. Under these oxidizing conditions, GSTU23 undergoes a structural change and forms a more favourable enzyme-substrate complex to overcome k<sub>cat</sub>
 decrease.</AbstractText>
<AbstractText Label="CONCLUSIONS AND SIGNIFICANCE">At lower H<sub>2</sub>
O<sub>2</sub>
 levels (100μM), GSTU23 forms methionine sulfoxides. Specifically, oxidation of Met14, located near the catalytic Ser13, could interfere with both GSH binding and catalytic activation. At higher H<sub>2</sub>
O<sub>2</sub>
 levels (200μM), the Cys65-Cys110 disulfide bond protects other cysteines and also methionines from overoxidation. This study shows the impact of oxidative stress on GSTU23 regulated by methionine sulfoxide reductases and glutaredoxin, and the mechanisms involved in maintaining its catalytic functionality under oxidizing conditions.</AbstractText>
<CopyrightInformation>Copyright © 2017 Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tossounian</LastName>
<ForeName>Maria-Armineh</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Van Molle</LastName>
<ForeName>Inge</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wahni</LastName>
<ForeName>Khadija</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jacques</LastName>
<ForeName>Silke</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium; VIB Center for Medical Biotechnology, B-9000 Ghent, Belgium; Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 927, B-9052 Ghent, Belgium; VIB Center for Plant Systems Biology, Technologiepark 927, B-9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gevaert</LastName>
<ForeName>Kris</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, Ghent University, B-9000 Ghent, Belgium; VIB Center for Medical Biotechnology, B-9000 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Van Breusegem</LastName>
<ForeName>Frank</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Department of Plant Biotechnology and Bioinformatics, Ghent University, Technologiepark 927, B-9052 Ghent, Belgium; VIB Center for Plant Systems Biology, Technologiepark 927, B-9052 Ghent, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Vertommen</LastName>
<ForeName>Didier</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>de Duve Institute, Université Catholique de Louvain, 1200 Brussels, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Young</LastName>
<ForeName>David</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rosado</LastName>
<ForeName>Leonardo Astolfi</ForeName>
<Initials>LA</Initials>
<AffiliationInfo><Affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Messens</LastName>
<ForeName>Joris</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>VIB-VUB Center for Structural Biology, B-1050 Brussels, Belgium; Brussels Center for Redox Biology, B-1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, B-1050 Brussels, Belgium. Electronic address: joris.messens@vib-vub.be.</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>2017</Year>
<Month>10</Month>
<Day>12</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="D004220">Disulfides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D020011">Protective Agents</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>AE28F7PNPL</RegistryNumber>
<NameOfSubstance UI="D008715">Methionine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>BBX060AN9V</RegistryNumber>
<NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber>
<NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>ULW86O013H</RegistryNumber>
<NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>XN1XVI4B2C</RegistryNumber>
<NameOfSubstance UI="C013111">methionine sulfoxide</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019803" MajorTopicYN="N">Glutathione Disulfide</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008715" MajorTopicYN="N">Methionine</DescriptorName>
<QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020011" MajorTopicYN="Y">Protective Agents</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Disulfide bond</Keyword>
<Keyword MajorTopicYN="Y">Glutathione transferase</Keyword>
<Keyword MajorTopicYN="Y">Kinetics</Keyword>
<Keyword MajorTopicYN="Y">Methionine sulfoxide</Keyword>
<Keyword MajorTopicYN="Y">Thermodynamics</Keyword>
<Keyword MajorTopicYN="Y">X-ray structure</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>06</Month>
<Day>13</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2017</Year>
<Month>10</Month>
<Day>04</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2017</Year>
<Month>10</Month>
<Day>10</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2017</Year>
<Month>10</Month>
<Day>17</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2018</Year>
<Month>11</Month>
<Day>2</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2017</Year>
<Month>10</Month>
<Day>17</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">29031766</ArticleId>
<ArticleId IdType="pii">S0304-4165(17)30328-8</ArticleId>
<ArticleId IdType="doi">10.1016/j.bbagen.2017.10.007</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Belgique</li>
</country>
<region><li>Province de Flandre-Orientale</li>
<li>Province du Brabant wallon</li>
<li>Région de Bruxelles-Capitale</li>
<li>Région flamande</li>
<li>Région wallonne</li>
</region>
<settlement><li>Bruxelles</li>
<li>Gand</li>
<li>Louvain-la-Neuve</li>
</settlement>
<orgName><li>Université catholique de Louvain</li>
<li>Université de Gand</li>
</orgName>
</list>
<tree><country name="Belgique"><noRegion><name sortKey="Tossounian, Maria Armineh" sort="Tossounian, Maria Armineh" uniqKey="Tossounian M" first="Maria-Armineh" last="Tossounian">Maria-Armineh Tossounian</name>
</noRegion>
<name sortKey="Gevaert, Kris" sort="Gevaert, Kris" uniqKey="Gevaert K" first="Kris" last="Gevaert">Kris Gevaert</name>
<name sortKey="Jacques, Silke" sort="Jacques, Silke" uniqKey="Jacques S" first="Silke" last="Jacques">Silke Jacques</name>
<name sortKey="Messens, Joris" sort="Messens, Joris" uniqKey="Messens J" first="Joris" last="Messens">Joris Messens</name>
<name sortKey="Rosado, Leonardo Astolfi" sort="Rosado, Leonardo Astolfi" uniqKey="Rosado L" first="Leonardo Astolfi" last="Rosado">Leonardo Astolfi Rosado</name>
<name sortKey="Van Breusegem, Frank" sort="Van Breusegem, Frank" uniqKey="Van Breusegem F" first="Frank" last="Van Breusegem">Frank Van Breusegem</name>
<name sortKey="Van Molle, Inge" sort="Van Molle, Inge" uniqKey="Van Molle I" first="Inge" last="Van Molle">Inge Van Molle</name>
<name sortKey="Vertommen, Didier" sort="Vertommen, Didier" uniqKey="Vertommen D" first="Didier" last="Vertommen">Didier Vertommen</name>
<name sortKey="Wahni, Khadija" sort="Wahni, Khadija" uniqKey="Wahni K" first="Khadija" last="Wahni">Khadija Wahni</name>
<name sortKey="Young, David" sort="Young, David" uniqKey="Young D" first="David" last="Young">David Young</name>
</country>
</tree>
</affiliations>
</record>

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Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.

Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.

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