Redox Conformation-Specific Protein-Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis.
Identifieur interne : 000024 ( Main/Exploration ); précédent : 000023; suivant : 000025Redox Conformation-Specific Protein-Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis.
Auteurs : Michael Liebthal [Allemagne] ; Johannes Schuetze [Allemagne] ; Anna Dreyer [Allemagne] ; Hans-Peter Mock [Allemagne] ; Karl-Josef Dietz [Allemagne]Source :
- Antioxidants (Basel, Switzerland) [ 2076-3921 ] ; 2020.
Abstract
2-Cysteine peroxiredoxins (2-CysPRX) are highly abundant thiol peroxidases in chloroplasts and play key roles in reactive oxygen species (ROS) defense and redox signaling. Peroxide-dependent oxidation of cysteines induces conformational changes that alter the ability for protein-protein interactions. For regeneration, 2-CysPRXs withdraw electrons from thioredoxins (TRXs) and participate in redox-dependent regulation by affecting the redox state of TRX-dependent targets, for example, in chloroplast metabolism. This work explores the redox conformation-specific 2-CysPRX interactome using an affinity-based pull down with recombinant variants arrested in specific quaternary conformations. This allowed us to address a critical and poorly explored aspect of the redox-regulatory network and showed that the interaction of TRXs, their interaction partners, and 2-CysPRX occur under contrasting redox conditions. A set of 178 chloroplast proteins were identified from leaf proteins and included proteins with functions in photosynthesis, carbohydrate, fatty acid and amino acid metabolism, and defense. These processes are known to be deregulated in plants devoid of 2-CysPRX. Selected enzymes like LIPOXYGENASE 2, CHLOROPLAST PROTEIN 12-1, CHORISMATE SYNTHASE, ß-CARBONIC ANHYDRASE, and FERREDOXIN-dependent GLUTAMATE SYNTHASE 1 were subjected to far Western, isothermal titration calorimetry, and enzyme assays for validation. The pull down fractions frequently contained TRXs as well as their target proteins, for example, FRUCTOSE-1,6-BISPHOSPHATASE and MALATE DEHYDROGENASE. The difference between TRX-dependent indirect interactions of TRX targets and 2-CysPRX and direct 2-CysPRX binding is hypothesized to be related to quaternary structure formation, where 2-CysPRX oligomers function as scaffold for complex formation, whereas TRX oxidase activity of 2-CysPRX controls the redox state of TRX-related enzyme activity.
DOI: 10.3390/antiox9060515
PubMed: 32545358
PubMed Central: PMC7346168
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Bielefeld</wicri:noRegion><wicri:noRegion>33615 Bielefeld</wicri:noRegion><wicri:noRegion>33615 Bielefeld</wicri:noRegion></affiliation></author><author><name sortKey="Schuetze, Johannes" sort="Schuetze, Johannes" uniqKey="Schuetze J" first="Johannes" last="Schuetze">Johannes Schuetze</name><affiliation wicri:level="1"><nlm:affiliation>Angewandte Biochemie, Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK), Corrensstraße 3, D-06466 Seeland, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Angewandte Biochemie, Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK), Corrensstraße 3, D-06466 Seeland</wicri:regionArea><wicri:noRegion>06466 Seeland</wicri:noRegion><wicri:noRegion>06466 Seeland</wicri:noRegion><wicri:noRegion>D-06466 Seeland</wicri:noRegion></affiliation></author><author><name sortKey="Dreyer, Anna" sort="Dreyer, Anna" uniqKey="Dreyer A" first="Anna" last="Dreyer">Anna Dreyer</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld</wicri:regionArea><wicri:noRegion>33615 Bielefeld</wicri:noRegion><wicri:noRegion>33615 Bielefeld</wicri:noRegion><wicri:noRegion>33615 Bielefeld</wicri:noRegion></affiliation></author><author><name sortKey="Mock, Hans Peter" sort="Mock, Hans Peter" uniqKey="Mock H" first="Hans-Peter" last="Mock">Hans-Peter Mock</name><affiliation wicri:level="1"><nlm:affiliation>Angewandte Biochemie, Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK), Corrensstraße 3, D-06466 Seeland, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Angewandte Biochemie, Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK), Corrensstraße 3, D-06466 Seeland</wicri:regionArea><wicri:noRegion>06466 Seeland</wicri:noRegion><wicri:noRegion>06466 Seeland</wicri:noRegion><wicri:noRegion>D-06466 Seeland</wicri:noRegion></affiliation></author><author><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld</wicri:regionArea><wicri:noRegion>33615 Bielefeld</wicri:noRegion><wicri:noRegion>33615 Bielefeld</wicri:noRegion><wicri:noRegion>33615 Bielefeld</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antioxidants (Basel, Switzerland)</title><idno type="ISSN">2076-3921</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">2-Cysteine peroxiredoxins (2-CysPRX) are highly abundant thiol peroxidases in chloroplasts and play key roles in reactive oxygen species (ROS) defense and redox signaling. Peroxide-dependent oxidation of cysteines induces conformational changes that alter the ability for protein-protein interactions. For regeneration, 2-CysPRXs withdraw electrons from thioredoxins (TRXs) and participate in redox-dependent regulation by affecting the redox state of TRX-dependent targets, for example, in chloroplast metabolism. This work explores the redox conformation-specific 2-CysPRX interactome using an affinity-based pull down with recombinant variants arrested in specific quaternary conformations. This allowed us to address a critical and poorly explored aspect of the redox-regulatory network and showed that the interaction of TRXs, their interaction partners, and 2-CysPRX occur under contrasting redox conditions. A set of 178 chloroplast proteins were identified from leaf proteins and included proteins with functions in photosynthesis, carbohydrate, fatty acid and amino acid metabolism, and defense. These processes are known to be deregulated in plants devoid of 2-CysPRX. Selected enzymes like LIPOXYGENASE 2, CHLOROPLAST PROTEIN 12-1, CHORISMATE SYNTHASE, ß-CARBONIC ANHYDRASE, and FERREDOXIN-dependent GLUTAMATE SYNTHASE 1 were subjected to far Western, isothermal titration calorimetry, and enzyme assays for validation. The pull down fractions frequently contained TRXs as well as their target proteins, for example, FRUCTOSE-1,6-BISPHOSPHATASE and MALATE DEHYDROGENASE. The difference between TRX-dependent indirect interactions of TRX targets and 2-CysPRX and direct 2-CysPRX binding is hypothesized to be related to quaternary structure formation, where 2-CysPRX oligomers function as scaffold for complex formation, whereas TRX oxidase activity of 2-CysPRX controls the redox state of TRX-related enzyme activity.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32545358</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2076-3921</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>6</Issue><PubDate><Year>2020</Year><Month>Jun</Month><Day>11</Day></PubDate></JournalIssue><Title>Antioxidants (Basel, Switzerland)</Title><ISOAbbreviation>Antioxidants (Basel)</ISOAbbreviation></Journal><ArticleTitle>Redox Conformation-Specific Protein-Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E515</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/antiox9060515</ELocationID><Abstract><AbstractText>2-Cysteine peroxiredoxins (2-CysPRX) are highly abundant thiol peroxidases in chloroplasts and play key roles in reactive oxygen species (ROS) defense and redox signaling. Peroxide-dependent oxidation of cysteines induces conformational changes that alter the ability for protein-protein interactions. For regeneration, 2-CysPRXs withdraw electrons from thioredoxins (TRXs) and participate in redox-dependent regulation by affecting the redox state of TRX-dependent targets, for example, in chloroplast metabolism. This work explores the redox conformation-specific 2-CysPRX interactome using an affinity-based pull down with recombinant variants arrested in specific quaternary conformations. This allowed us to address a critical and poorly explored aspect of the redox-regulatory network and showed that the interaction of TRXs, their interaction partners, and 2-CysPRX occur under contrasting redox conditions. A set of 178 chloroplast proteins were identified from leaf proteins and included proteins with functions in photosynthesis, carbohydrate, fatty acid and amino acid metabolism, and defense. These processes are known to be deregulated in plants devoid of 2-CysPRX. Selected enzymes like LIPOXYGENASE 2, CHLOROPLAST PROTEIN 12-1, CHORISMATE SYNTHASE, ß-CARBONIC ANHYDRASE, and FERREDOXIN-dependent GLUTAMATE SYNTHASE 1 were subjected to far Western, isothermal titration calorimetry, and enzyme assays for validation. The pull down fractions frequently contained TRXs as well as their target proteins, for example, FRUCTOSE-1,6-BISPHOSPHATASE and MALATE DEHYDROGENASE. The difference between TRX-dependent indirect interactions of TRX targets and 2-CysPRX and direct 2-CysPRX binding is hypothesized to be related to quaternary structure formation, where 2-CysPRX oligomers function as scaffold for complex formation, whereas TRX oxidase activity of 2-CysPRX controls the redox state of TRX-related enzyme activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liebthal</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schuetze</LastName><ForeName>Johannes</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Angewandte Biochemie, Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK), Corrensstraße 3, D-06466 Seeland, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dreyer</LastName><ForeName>Anna</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mock</LastName><ForeName>Hans-Peter</ForeName><Initials>HP</Initials><AffiliationInfo><Affiliation>Angewandte Biochemie, Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung (IPK), Corrensstraße 3, D-06466 Seeland, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dietz</LastName><ForeName>Karl-Josef</ForeName><Initials>KJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, 33615 Bielefeld, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>DI 346/17&18; MO 479/11-2</GrantID><Agency>Deutsche Forschungsgemeinschaft</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>06</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Antioxidants (Basel)</MedlineTA><NlmUniqueID>101668981</NlmUniqueID><ISSNLinking>2076-3921</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">2-cysteine peroxiredoxin</Keyword><Keyword MajorTopicYN="N">interactome</Keyword><Keyword MajorTopicYN="N">proteomics</Keyword><Keyword MajorTopicYN="N">redox</Keyword><Keyword MajorTopicYN="N">thiol</Keyword><Keyword MajorTopicYN="N">thioredoxin</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>05</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>06</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>06</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>6</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>6</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>18</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32545358</ArticleId><ArticleId IdType="pii">antiox9060515</ArticleId><ArticleId IdType="doi">10.3390/antiox9060515</ArticleId><ArticleId 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first="Hans-Peter" last="Mock">Hans-Peter Mock</name><name sortKey="Schuetze, Johannes" sort="Schuetze, Johannes" uniqKey="Schuetze J" first="Johannes" last="Schuetze">Johannes Schuetze</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Redox Conformation-Specific Protein-Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis.
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