Thiol Based Redox Signaling in Plant Nucleus.
Identifieur interne : 000203 ( Main/Exploration ); précédent : 000202; suivant : 000204Thiol Based Redox Signaling in Plant Nucleus.
Auteurs : Laura Martins [France] ; José Abraham Trujillo-Hernandez [France] ; Jean-Philippe Reichheld [France]Source :
- Frontiers in plant science [ 1664-462X ] ; 2018.
Abstract
Reactive oxygen species (ROS) are well-described by-products of cellular metabolic activities, acting as signaling molecules and regulating the redox state of proteins. Solvent exposed thiol residues like cysteines are particularly sensitive to oxidation and their redox state affects structural and biochemical capacities of many proteins. While thiol redox regulation has been largely studied in several cell compartments like in the plant chloroplast, little is known about redox sensitive proteins in the nucleus. Recent works have revealed that proteins with oxidizable thiols are important for the regulation of many nuclear functions, including gene expression, transcription, epigenetics, and chromatin remodeling. Moreover, thiol reducing molecules like glutathione and specific isoforms of thiols reductases, thioredoxins and glutaredoxins were found in different nuclear subcompartments, further supporting that thiol-dependent systems are active in the nucleus. This mini-review aims to discuss recent progress in plant thiol redox field, taking examples of redox regulated nuclear proteins and focusing on major thiol redox systems acting in the nucleus.
DOI: 10.3389/fpls.2018.00705
PubMed: 29892308
PubMed Central: PMC5985474
Affiliations:
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des Plantes, Université Perpignan Via Domitia, Perpignan, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, Perpignan</wicri:regionArea><placeName><region type="region">Occitanie (région administrative)</region><region type="old region">Languedoc-Roussillon</region><settlement type="city">Perpignan</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:affiliation>Laboratoire Génome et Développement des Plantes, Centre National de la Recherche Scientifique, Perpignan, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Génome et Développement des Plantes, Centre National de la Recherche Scientifique, Perpignan</wicri:regionArea><placeName><region type="region">Occitanie (région administrative)</region><region type="old region">Languedoc-Roussillon</region><settlement 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type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reactive oxygen species (ROS) are well-described by-products of cellular metabolic activities, acting as signaling molecules and regulating the redox state of proteins. Solvent exposed thiol residues like cysteines are particularly sensitive to oxidation and their redox state affects structural and biochemical capacities of many proteins. While thiol redox regulation has been largely studied in several cell compartments like in the plant chloroplast, little is known about redox sensitive proteins in the nucleus. Recent works have revealed that proteins with oxidizable thiols are important for the regulation of many nuclear functions, including gene expression, transcription, epigenetics, and chromatin remodeling. Moreover, thiol reducing molecules like glutathione and specific isoforms of thiols reductases, thioredoxins and glutaredoxins were found in different nuclear subcompartments, further supporting that thiol-dependent systems are active in the nucleus. This mini-review aims to discuss recent progress in plant thiol redox field, taking examples of redox regulated nuclear proteins and focusing on major thiol redox systems acting in the nucleus.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">29892308</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Thiol Based Redox Signaling in Plant Nucleus.</ArticleTitle><Pagination><MedlinePgn>705</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2018.00705</ELocationID><Abstract><AbstractText>Reactive oxygen species (ROS) are well-described by-products of cellular metabolic activities, acting as signaling molecules and regulating the redox state of proteins. Solvent exposed thiol residues like cysteines are particularly sensitive to oxidation and their redox state affects structural and biochemical capacities of many proteins. While thiol redox regulation has been largely studied in several cell compartments like in the plant chloroplast, little is known about redox sensitive proteins in the nucleus. Recent works have revealed that proteins with oxidizable thiols are important for the regulation of many nuclear functions, including gene expression, transcription, epigenetics, and chromatin remodeling. Moreover, thiol reducing molecules like glutathione and specific isoforms of thiols reductases, thioredoxins and glutaredoxins were found in different nuclear subcompartments, further supporting that thiol-dependent systems are active in the nucleus. This mini-review aims to discuss recent progress in plant thiol redox field, taking examples of redox regulated nuclear proteins and focusing on major thiol redox systems acting in the nucleus.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Martins</LastName><ForeName>Laura</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, Perpignan, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Centre National de la Recherche Scientifique, Perpignan, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Trujillo-Hernandez</LastName><ForeName>José Abraham</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Université Perpignan Via Domitia, Perpignan, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Centre National de la Recherche Scientifique, Perpignan, France.</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, Perpignan, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, Centre National de la Recherche Scientifique, Perpignan, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Plant Sci</MedlineTA><NlmUniqueID>101568200</NlmUniqueID><ISSNLinking>1664-462X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ROS</Keyword><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>2018</Year><Month>02</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>05</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>6</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name><name sortKey="Reichheld, Jean Philippe" sort="Reichheld, Jean Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name><name sortKey="Trujillo Hernandez, Jose Abraham" sort="Trujillo Hernandez, Jose Abraham" uniqKey="Trujillo Hernandez J" first="José Abraham" last="Trujillo-Hernandez">José Abraham Trujillo-Hernandez</name><name sortKey="Trujillo Hernandez, Jose Abraham" sort="Trujillo Hernandez, Jose Abraham" uniqKey="Trujillo Hernandez J" first="José Abraham" last="Trujillo-Hernandez">José Abraham Trujillo-Hernandez</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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