Nuclear thiol redox systems in plants.
Identifieur interne : 000437 ( Main/Exploration ); précédent : 000436; suivant : 000438Nuclear thiol redox systems in plants.
Auteurs : Valérie Delorme-Hinoux [France] ; Sajid A K. Bangash [Allemagne] ; Andreas J. Meyer [Allemagne] ; Jean-Philippe Reichheld [France]Source :
- Plant science : an international journal of experimental plant biology [ 1873-2259 ] ; 2016.
Descripteurs français
- KwdFr :
- Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Isoformes de protéines (génétique), Isoformes de protéines (métabolisme), Noyau de la cellule (métabolisme), Oxydoréduction (MeSH), Plantes (enzymologie), Plantes (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Thiols (métabolisme), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
- enzymologie : Plantes.
- génétique : Glutarédoxines, Isoformes de protéines, Protéines végétales, Thiorédoxines.
- métabolisme : Glutarédoxines, Glutathion, Isoformes de protéines, Noyau de la cellule, Plantes, Protéines végétales, Thiols, Thiorédoxines.
- Oxydoréduction.
English descriptors
- KwdEn :
- Cell Nucleus (metabolism), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Oxidation-Reduction (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism), Plants (enzymology), Plants (metabolism), Protein Isoforms (genetics), Protein Isoforms (metabolism), Sulfhydryl Compounds (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism).
- MESH :
- chemical , genetics : Glutaredoxins, Plant Proteins, Protein Isoforms, Thioredoxins.
- enzymology : Plants.
- metabolism : Cell Nucleus, Glutaredoxins, Glutathione, Plant Proteins, Plants, Protein Isoforms, Sulfhydryl Compounds, Thioredoxins.
- Oxidation-Reduction.
Abstract
Thiol-disulfide redox regulation is essential for many cellular functions in plants. It has major roles in defense mechanisms, maintains the redox status of the cell and plays structural, with regulatory roles for many proteins. Although thiol-based redox regulation has been extensively studied in subcellular organelles such as chloroplasts, it has been much less studied in the nucleus. Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems. We first focus on the functions of glutathione in the nucleus and discuss recent data concerning accumulation of glutathione in the nucleus. We also provide evidence that glutathione reduction is potentially active in the nucleus. Recent data suggests that the nucleus is enriched in specific GRX and TRX isoforms. We discuss the biochemical and molecular characteristics of these isoforms and focus on genetic evidences for their potential nuclear functions. Finally, we make an overview of the different thiol-based redox regulated proteins in the nucleus. These proteins are involved in various pathways including transcriptional regulation, metabolism and signaling.
DOI: 10.1016/j.plantsci.2015.12.002
PubMed: 26795153
Affiliations:
- Allemagne, France
- District de Cologne, Languedoc-Roussillon, Occitanie (région administrative), Rhénanie-du-Nord-Westphalie
- Bonn, Perpignan
Links toward previous steps (curation, corpus...)
Le document en format XML
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Electronic address: valerie.hinoux@univ-perp.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, F-66860 Perpignan, France; Laboratoire Génome et Développement des Plantes, CNRS, F-66860 Perpignan</wicri:regionArea><placeName><region type="region" nuts="2">Occitanie (région administrative)</region><region type="old region" nuts="2">Languedoc-Roussillon</region><settlement type="city">Perpignan</settlement></placeName></affiliation></author><author><name sortKey="Bangash, Sajid A K" sort="Bangash, Sajid A K" uniqKey="Bangash S" first="Sajid A K" last="Bangash">Sajid A K. Bangash</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="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. 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="Reichheld, Jean Philippe" sort="Reichheld, Jean Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, F-66860 Perpignan, France; Laboratoire Génome et Développement des Plantes, CNRS, F-66860 Perpignan, France. Electronic address: jpr@univ-perp.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, F-66860 Perpignan, France; Laboratoire Génome et Développement des Plantes, CNRS, F-66860 Perpignan</wicri:regionArea><placeName><region type="region" nuts="2">Occitanie (région administrative)</region><region type="old region" nuts="2">Languedoc-Roussillon</region><settlement type="city">Perpignan</settlement></placeName></affiliation></author></analytic><series><title level="j">Plant science : an international journal of experimental plant biology</title><idno type="eISSN">1873-2259</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Nucleus (metabolism)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Plants (enzymology)</term><term>Plants (metabolism)</term><term>Protein Isoforms (genetics)</term><term>Protein Isoforms (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Isoformes de protéines (génétique)</term><term>Isoformes de protéines (métabolisme)</term><term>Noyau de la cellule (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Plantes (enzymologie)</term><term>Plantes (métabolisme)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term><term>Thiols (métabolisme)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Plant Proteins</term><term>Protein Isoforms</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plantes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Isoformes de protéines</term><term>Protéines végétales</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Glutaredoxins</term><term>Glutathione</term><term>Plant Proteins</term><term>Plants</term><term>Protein Isoforms</term><term>Sulfhydryl Compounds</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term><term>Isoformes de protéines</term><term>Noyau de la cellule</term><term>Plantes</term><term>Protéines végétales</term><term>Thiols</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thiol-disulfide redox regulation is essential for many cellular functions in plants. It has major roles in defense mechanisms, maintains the redox status of the cell and plays structural, with regulatory roles for many proteins. Although thiol-based redox regulation has been extensively studied in subcellular organelles such as chloroplasts, it has been much less studied in the nucleus. Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems. We first focus on the functions of glutathione in the nucleus and discuss recent data concerning accumulation of glutathione in the nucleus. We also provide evidence that glutathione reduction is potentially active in the nucleus. Recent data suggests that the nucleus is enriched in specific GRX and TRX isoforms. We discuss the biochemical and molecular characteristics of these isoforms and focus on genetic evidences for their potential nuclear functions. Finally, we make an overview of the different thiol-based redox regulated proteins in the nucleus. These proteins are involved in various pathways including transcriptional regulation, metabolism and signaling. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26795153</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2259</ISSN><JournalIssue CitedMedium="Internet"><Volume>243</Volume><PubDate><Year>2016</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Plant science : an international journal of experimental plant biology</Title><ISOAbbreviation>Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Nuclear thiol redox systems in plants.</ArticleTitle><Pagination><MedlinePgn>84-95</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.plantsci.2015.12.002</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0168-9452(15)30112-6</ELocationID><Abstract><AbstractText>Thiol-disulfide redox regulation is essential for many cellular functions in plants. It has major roles in defense mechanisms, maintains the redox status of the cell and plays structural, with regulatory roles for many proteins. Although thiol-based redox regulation has been extensively studied in subcellular organelles such as chloroplasts, it has been much less studied in the nucleus. Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems. We first focus on the functions of glutathione in the nucleus and discuss recent data concerning accumulation of glutathione in the nucleus. We also provide evidence that glutathione reduction is potentially active in the nucleus. Recent data suggests that the nucleus is enriched in specific GRX and TRX isoforms. We discuss the biochemical and molecular characteristics of these isoforms and focus on genetic evidences for their potential nuclear functions. Finally, we make an overview of the different thiol-based redox regulated proteins in the nucleus. These proteins are involved in various pathways including transcriptional regulation, metabolism and signaling. </AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Ireland Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Delorme-Hinoux</LastName><ForeName>Valérie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, F-66860 Perpignan, France; Laboratoire Génome et Développement des Plantes, CNRS, F-66860 Perpignan, France. Electronic address: valerie.hinoux@univ-perp.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bangash</LastName><ForeName>Sajid A K</ForeName><Initials>SA</Initials><AffiliationInfo><Affiliation>INRES-Chemical Signalling, University of Bonn, Friedrich-Ebert-Allee 144, 53113 Bonn, Germany.</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>Reichheld</LastName><ForeName>Jean-Philippe</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, F-66860 Perpignan, France; Laboratoire Génome et Développement des Plantes, CNRS, F-66860 Perpignan, France. Electronic address: jpr@univ-perp.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><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>12</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>Ireland</Country><MedlineTA>Plant Sci</MedlineTA><NlmUniqueID>9882015</NlmUniqueID><ISSNLinking>0168-9452</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Glutathione</Keyword><Keyword MajorTopicYN="N">Nucleus</Keyword><Keyword MajorTopicYN="N">Thiol</Keyword><Keyword MajorTopicYN="N">Thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>10</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>12</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>12</Month><Day>07</Day></PubMedPubDate><PubMedPubDate 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administrative)"><name sortKey="Delorme Hinoux, Valerie" sort="Delorme Hinoux, Valerie" uniqKey="Delorme Hinoux V" first="Valérie" last="Delorme-Hinoux">Valérie Delorme-Hinoux</name></region><name sortKey="Reichheld, Jean Philippe" sort="Reichheld, Jean Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name></country><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Bangash, Sajid A K" sort="Bangash, Sajid A K" uniqKey="Bangash S" first="Sajid A K" last="Bangash">Sajid A K. Bangash</name></region><name sortKey="Meyer, Andreas J" sort="Meyer, Andreas J" uniqKey="Meyer A" first="Andreas J" last="Meyer">Andreas J. Meyer</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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