Multilevel regulation of non-photochemical quenching and state transitions by chloroplast NADPH-dependent thioredoxin reductase.
Identifieur interne : 000154 ( Main/Exploration ); précédent : 000153; suivant : 000155Multilevel regulation of non-photochemical quenching and state transitions by chloroplast NADPH-dependent thioredoxin reductase.
Auteurs : Lauri Nikkanen [Finlande] ; Manuel Guinea Diaz [Finlande] ; Jouni Toivola [Finlande] ; Arjun Tiwari [Finlande] ; Eevi Rintam Ki [Finlande]Source :
- Physiologia plantarum [ 1399-3054 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Chloroplastes, Complexe protéique du photosystème I, Complexe protéique du photosystème II, NADP, Thioredoxin-disulfide reductase.
- physiologie : Photosynthèse.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : NADP, Photosystem I Protein Complex, Photosystem II Protein Complex, Thioredoxin-Disulfide Reductase.
- metabolism : Chloroplasts.
- physiology : Photosynthesis.
Abstract
In natural growth habitats, plants face constant, unpredictable changes in light conditions. To avoid damage to the photosynthetic apparatus on thylakoid membranes in chloroplasts, and to avoid wasteful reactions, it is crucial to maintain a redox balance both within the components of photosynthetic electron transfer chain and between the light reactions and stromal carbon metabolism under fluctuating light conditions. This requires coordinated function of the photoprotective and regulatory mechanisms, such as non-photochemical quenching (NPQ) and reversible redistribution of excitation energy between photosystem II (PSII) and photosystem I (PSI). In this paper, we show that the NADPH-dependent chloroplast thioredoxin system (NTRC) is involved in the control of the activation of these mechanisms. In plants with altered NTRC content, the strict correlation between lumenal pH and NPQ is partially lost. We propose that NTRC contributes to downregulation of a slow-relaxing constituent of NPQ, whose induction is independent of lumenal acidification. Additionally, overexpression of NTRC enhances the ability to adjust the excitation balance between PSII and PSI, and improves the ability to oxidize the electron transfer chain during changes in light conditions. Thiol regulation allows coupling of the electron transfer chain to the stromal redox state during these changes.
DOI: 10.1111/ppl.12914
PubMed: 30578537
PubMed Central: PMC6850073
Affiliations:
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sort="Guinea Diaz, Manuel" uniqKey="Guinea Diaz M" first="Manuel" last="Guinea Diaz">Manuel Guinea Diaz</name><affiliation wicri:level="4"><nlm:affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku</wicri:regionArea><placeName><settlement type="city">Turku</settlement><region type="région" nuts="2">Finlande occidentale</region></placeName><orgName type="university">Université de Turku</orgName></affiliation></author><author><name sortKey="Toivola, Jouni" sort="Toivola, Jouni" uniqKey="Toivola J" first="Jouni" last="Toivola">Jouni Toivola</name><affiliation wicri:level="4"><nlm:affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Molecular Plant Biology, 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first="Eevi" last="Rintam Ki">Eevi Rintam Ki</name><affiliation wicri:level="4"><nlm:affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku</wicri:regionArea><placeName><settlement type="city">Turku</settlement><region type="région" nuts="2">Finlande occidentale</region></placeName><orgName type="university">Université de Turku</orgName></affiliation></author></analytic><series><title level="j">Physiologia plantarum</title><idno type="eISSN">1399-3054</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chloroplasts (metabolism)</term><term>NADP (metabolism)</term><term>Photosynthesis (physiology)</term><term>Photosystem I Protein Complex (metabolism)</term><term>Photosystem II Protein Complex (metabolism)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chloroplastes (métabolisme)</term><term>Complexe protéique du photosystème I (métabolisme)</term><term>Complexe protéique du photosystème II (métabolisme)</term><term>NADP (métabolisme)</term><term>Photosynthèse (physiologie)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>NADP</term><term>Photosystem I Protein Complex</term><term>Photosystem II Protein Complex</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Chloroplasts</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Chloroplastes</term><term>Complexe protéique du photosystème I</term><term>Complexe protéique du photosystème II</term><term>NADP</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Photosynthèse</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Photosynthesis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In natural growth habitats, plants face constant, unpredictable changes in light conditions. To avoid damage to the photosynthetic apparatus on thylakoid membranes in chloroplasts, and to avoid wasteful reactions, it is crucial to maintain a redox balance both within the components of photosynthetic electron transfer chain and between the light reactions and stromal carbon metabolism under fluctuating light conditions. This requires coordinated function of the photoprotective and regulatory mechanisms, such as non-photochemical quenching (NPQ) and reversible redistribution of excitation energy between photosystem II (PSII) and photosystem I (PSI). In this paper, we show that the NADPH-dependent chloroplast thioredoxin system (NTRC) is involved in the control of the activation of these mechanisms. In plants with altered NTRC content, the strict correlation between lumenal pH and NPQ is partially lost. We propose that NTRC contributes to downregulation of a slow-relaxing constituent of NPQ, whose induction is independent of lumenal acidification. Additionally, overexpression of NTRC enhances the ability to adjust the excitation balance between PSII and PSI, and improves the ability to oxidize the electron transfer chain during changes in light conditions. Thiol regulation allows coupling of the electron transfer chain to the stromal redox state during these changes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30578537</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-3054</ISSN><JournalIssue CitedMedium="Internet"><Volume>166</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>May</Month></PubDate></JournalIssue><Title>Physiologia plantarum</Title><ISOAbbreviation>Physiol Plant</ISOAbbreviation></Journal><ArticleTitle>Multilevel regulation of non-photochemical quenching and state transitions by chloroplast NADPH-dependent thioredoxin reductase.</ArticleTitle><Pagination><MedlinePgn>211-225</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/ppl.12914</ELocationID><Abstract><AbstractText>In natural growth habitats, plants face constant, unpredictable changes in light conditions. To avoid damage to the photosynthetic apparatus on thylakoid membranes in chloroplasts, and to avoid wasteful reactions, it is crucial to maintain a redox balance both within the components of photosynthetic electron transfer chain and between the light reactions and stromal carbon metabolism under fluctuating light conditions. This requires coordinated function of the photoprotective and regulatory mechanisms, such as non-photochemical quenching (NPQ) and reversible redistribution of excitation energy between photosystem II (PSII) and photosystem I (PSI). In this paper, we show that the NADPH-dependent chloroplast thioredoxin system (NTRC) is involved in the control of the activation of these mechanisms. In plants with altered NTRC content, the strict correlation between lumenal pH and NPQ is partially lost. We propose that NTRC contributes to downregulation of a slow-relaxing constituent of NPQ, whose induction is independent of lumenal acidification. Additionally, overexpression of NTRC enhances the ability to adjust the excitation balance between PSII and PSI, and improves the ability to oxidize the electron transfer chain during changes in light conditions. Thiol regulation allows coupling of the electron transfer chain to the stromal redox state during these changes.</AbstractText><CopyrightInformation>© 2018 The Authors. Physiologia Plantarum published by John Wiley & Sons Ltd on behalf of Scandinavian Plant Physiology Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nikkanen</LastName><ForeName>Lauri</ForeName><Initials>L</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-7192-9322</Identifier><AffiliationInfo><Affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guinea Diaz</LastName><ForeName>Manuel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Toivola</LastName><ForeName>Jouni</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tiwari</LastName><ForeName>Arjun</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rintamäki</LastName><ForeName>Eevi</ForeName><Initials>E</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-1353-3995</Identifier><AffiliationInfo><Affiliation>Molecular Plant Biology, Department of Biochemistry, University of Turku, Turku, Finland.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>276392</GrantID><Agency>Academy of Finland Grants</Agency><Country></Country></Grant><Grant><GrantID>307335</GrantID><Agency>Academy of Finland Grants</Agency><Country></Country></Grant><Grant><GrantID>Doctoral program in molecular life sciences</GrantID><Agency>University of Turku Graduate School</Agency><Country></Country></Grant><Grant><Agency>Doctoral Program in Molecular Life Sciences in the University of Turku Graduate School</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>02</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Physiol Plant</MedlineTA><NlmUniqueID>1256322</NlmUniqueID><ISSNLinking>0031-9317</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D045331">Photosystem I Protein Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D045332">Photosystem II Protein Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010788" MajorTopicYN="N">Photosynthesis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045331" MajorTopicYN="N">Photosystem I Protein Complex</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045332" MajorTopicYN="N">Photosystem II Protein Complex</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>10</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>12</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>12</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>12</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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name="Finlande"><region name="Finlande occidentale"><name sortKey="Nikkanen, Lauri" sort="Nikkanen, Lauri" uniqKey="Nikkanen L" first="Lauri" last="Nikkanen">Lauri Nikkanen</name></region><name sortKey="Guinea Diaz, Manuel" sort="Guinea Diaz, Manuel" uniqKey="Guinea Diaz M" first="Manuel" last="Guinea Diaz">Manuel Guinea Diaz</name><name sortKey="Rintam Ki, Eevi" sort="Rintam Ki, Eevi" uniqKey="Rintam Ki E" first="Eevi" last="Rintam Ki">Eevi Rintam Ki</name><name sortKey="Tiwari, Arjun" sort="Tiwari, Arjun" uniqKey="Tiwari A" first="Arjun" last="Tiwari">Arjun Tiwari</name><name sortKey="Toivola, Jouni" sort="Toivola, Jouni" uniqKey="Toivola J" first="Jouni" last="Toivola">Jouni Toivola</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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