Redox regulation by peroxiredoxins is linked to their thioredoxin-dependent oxidase function.
Identifieur interne : 000023 ( Main/Exploration ); précédent : 000022; suivant : 000024Redox regulation by peroxiredoxins is linked to their thioredoxin-dependent oxidase function.
Auteurs : Wilena Telman [Allemagne] ; Michael Liebthal [Allemagne] ; Karl-Josef Dietz [Allemagne]Source :
- Photosynthesis research [ 1573-5079 ] ; 2020.
Abstract
The chloroplast contains three types of peroxiredoxins (PRXs). Recently, 2-CysPRX was associated with thioredoxin (TRX) oxidation-dependent redox regulation. Here, this analysis was expanded to include PRXQ and PRXIIE. Oxidized PRXQ was able to inactivate NADPH malate dehydrogenase and fructose-1,6-bisphosphatase most efficiently in the presence of TRX-m1 and TRX-m4. The inactivation ability of TRXs did not entirely match their reductive activation efficiency. PRXIIE was unable to function as TRX oxidase in enzyme regulation. This conclusion was further supported by the observation that PRXQ adopts the oxidized form by about 50% in leaves, supporting a possible function as a TRX oxidase similar to 2-CysPRX. Results on the oxidation state of photosystem I (P700), plastocyanin, and ferredoxin in intact leaves indicate that each type of PRX has distinct regulatory functions, and that both 2-CysPRX and PRXQ conditionally assist in adjusting the redox state of target proteins for proper activity.
DOI: 10.1007/s11120-019-00691-0
PubMed: 31768716
Affiliations:
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Michael" uniqKey="Liebthal M" first="Michael" last="Liebthal">Michael Liebthal</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 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, University Str. 25, 33615, Bielefeld</wicri:regionArea><wicri:noRegion>33615, Bielefeld</wicri:noRegion><wicri:noRegion>33615, Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</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, University Str. 25, 33615, Bielefeld, Germany. karl-josef.dietz@uni-bielefeld.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 33615, Bielefeld</wicri:regionArea><wicri:noRegion>33615, Bielefeld</wicri:noRegion><wicri:noRegion>33615, Bielefeld</wicri:noRegion><wicri:noRegion>Bielefeld</wicri:noRegion></affiliation></author></analytic><series><title level="j">Photosynthesis research</title><idno type="eISSN">1573-5079</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">The chloroplast contains three types of peroxiredoxins (PRXs). Recently, 2-CysPRX was associated with thioredoxin (TRX) oxidation-dependent redox regulation. Here, this analysis was expanded to include PRXQ and PRXIIE. Oxidized PRXQ was able to inactivate NADPH malate dehydrogenase and fructose-1,6-bisphosphatase most efficiently in the presence of TRX-m1 and TRX-m4. The inactivation ability of TRXs did not entirely match their reductive activation efficiency. PRXIIE was unable to function as TRX oxidase in enzyme regulation. This conclusion was further supported by the observation that PRXQ adopts the oxidized form by about 50% in leaves, supporting a possible function as a TRX oxidase similar to 2-CysPRX. Results on the oxidation state of photosystem I (P700), plastocyanin, and ferredoxin in intact leaves indicate that each type of PRX has distinct regulatory functions, and that both 2-CysPRX and PRXQ conditionally assist in adjusting the redox state of target proteins for proper activity.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">31768716</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-5079</ISSN><JournalIssue CitedMedium="Internet"><Volume>145</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Photosynthesis research</Title><ISOAbbreviation>Photosynth Res</ISOAbbreviation></Journal><ArticleTitle>Redox regulation by peroxiredoxins is linked to their thioredoxin-dependent oxidase function.</ArticleTitle><Pagination><MedlinePgn>31-41</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11120-019-00691-0</ELocationID><Abstract><AbstractText>The chloroplast contains three types of peroxiredoxins (PRXs). Recently, 2-CysPRX was associated with thioredoxin (TRX) oxidation-dependent redox regulation. Here, this analysis was expanded to include PRXQ and PRXIIE. Oxidized PRXQ was able to inactivate NADPH malate dehydrogenase and fructose-1,6-bisphosphatase most efficiently in the presence of TRX-m1 and TRX-m4. The inactivation ability of TRXs did not entirely match their reductive activation efficiency. PRXIIE was unable to function as TRX oxidase in enzyme regulation. This conclusion was further supported by the observation that PRXQ adopts the oxidized form by about 50% in leaves, supporting a possible function as a TRX oxidase similar to 2-CysPRX. Results on the oxidation state of photosystem I (P700), plastocyanin, and ferredoxin in intact leaves indicate that each type of PRX has distinct regulatory functions, and that both 2-CysPRX and PRXQ conditionally assist in adjusting the redox state of target proteins for proper activity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Telman</LastName><ForeName>Wilena</ForeName><Initials>W</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-6336-486X</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 33615, Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liebthal</LastName><ForeName>Michael</ForeName><Initials>M</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-3198-0358</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 33615, Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dietz</LastName><ForeName>Karl-Josef</ForeName><Initials>KJ</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-0311-2182</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, University Str. 25, 33615, Bielefeld, Germany. karl-josef.dietz@uni-bielefeld.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Photosynth Res</MedlineTA><NlmUniqueID>100954728</NlmUniqueID><ISSNLinking>0166-8595</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">A. thaliana</Keyword><Keyword MajorTopicYN="N">Calvin–Benson cycle</Keyword><Keyword MajorTopicYN="N">Malate valve</Keyword><Keyword MajorTopicYN="N">Peroxiredoxins</Keyword><Keyword MajorTopicYN="N">Redox regulation</Keyword><Keyword MajorTopicYN="N">Thioredoxins</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>07</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>11</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>11</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>11</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>11</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31768716</ArticleId><ArticleId IdType="doi">10.1007/s11120-019-00691-0</ArticleId><ArticleId IdType="pii">10.1007/s11120-019-00691-0</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Telman, Wilena" sort="Telman, Wilena" uniqKey="Telman W" first="Wilena" last="Telman">Wilena Telman</name></noRegion><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name><name sortKey="Liebthal, Michael" sort="Liebthal, Michael" uniqKey="Liebthal M" first="Michael" last="Liebthal">Michael Liebthal</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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