Malate valves: old shuttles with new perspectives.
Identifieur interne : 000114 ( Main/Exploration ); précédent : 000113; suivant : 000115Malate valves: old shuttles with new perspectives.
Auteurs : J. Selinski [Australie] ; R. Scheibe [Allemagne]Source :
- Plant biology (Stuttgart, Germany) [ 1438-8677 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Chloroplastes, Malate dehydrogenase, Malates, NAD.
- Famille multigénique, Respiration cellulaire.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Malate Dehydrogenase, Malates, NAD.
- metabolism : Chloroplasts.
- Cell Respiration, Multigene Family.
Abstract
Malate valves act as powerful systems for balancing the ATP/NAD(P)H ratio required in various subcellular compartments in plant cells. As components of malate valves, isoforms of malate dehydrogenases (MDHs) and dicarboxylate translocators catalyse the reversible interconversion of malate and oxaloacetate and their transport. Depending on the co-enzyme specificity of the MDH isoforms, either NADH or NADPH can be transported indirectly. Arabidopsis thaliana possesses nine genes encoding MDH isoenzymes. Activities of NAD-dependent MDHs have been detected in mitochondria, peroxisomes, cytosol and plastids. In addition, chloroplasts possess a NADP-dependent MDH isoform. The NADP-MDH as part of the 'light malate valve' plays an important role as a poising mechanism to adjust the ATP/NADPH ratio in the stroma. Its activity is strictly regulated by post-translational redox-modification mediated via the ferredoxin-thioredoxin system and fine control via the NADP+ /NADP(H) ratio, thereby maintaining redox homeostasis under changing conditions. In contrast, the plastid NAD-MDH ('dark malate valve') is constitutively active and its lack leads to failure in early embryo development. While redox regulation of the main cytosolic MDH isoform has been shown, knowledge about regulation of the other two cytosolic MDHs as well as NAD-MDH isoforms from peroxisomes and mitochondria is still lacking. Knockout mutants lacking the isoforms from chloroplasts, mitochondria and peroxisomes have been characterised, but not much is known about cytosolic NAD-MDH isoforms and their role in planta. This review updates the current knowledge on MDH isoforms and the shuttle systems for intercompartmental dicarboxylate exchange, focusing on the various metabolic functions of these valves.
DOI: 10.1111/plb.12869
PubMed: 29933514
PubMed Central: PMC6586076
Affiliations:
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Scheibe</name><affiliation wicri:level="1"><nlm:affiliation>Division of Plant Physiology, Department of Biology/Chemistry, University of Osnabrueck, Osnabrueck, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Division of Plant Physiology, Department of Biology/Chemistry, University of Osnabrueck, Osnabrueck</wicri:regionArea><wicri:noRegion>Osnabrueck</wicri:noRegion><wicri:noRegion>Osnabrueck</wicri:noRegion><wicri:noRegion>Osnabrueck</wicri:noRegion></affiliation></author></analytic><series><title level="j">Plant biology (Stuttgart, Germany)</title><idno type="eISSN">1438-8677</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Respiration (MeSH)</term><term>Chloroplasts (metabolism)</term><term>Malate Dehydrogenase (metabolism)</term><term>Malates (metabolism)</term><term>Multigene Family (MeSH)</term><term>NAD (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chloroplastes (métabolisme)</term><term>Famille multigénique (MeSH)</term><term>Malate dehydrogenase (métabolisme)</term><term>Malates (métabolisme)</term><term>NAD (métabolisme)</term><term>Respiration cellulaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Malate Dehydrogenase</term><term>Malates</term><term>NAD</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>Malate dehydrogenase</term><term>Malates</term><term>NAD</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Respiration</term><term>Multigene Family</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Famille multigénique</term><term>Respiration cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Malate valves act as powerful systems for balancing the ATP/NAD(P)H ratio required in various subcellular compartments in plant cells. As components of malate valves, isoforms of malate dehydrogenases (MDHs) and dicarboxylate translocators catalyse the reversible interconversion of malate and oxaloacetate and their transport. Depending on the co-enzyme specificity of the MDH isoforms, either NADH or NADPH can be transported indirectly. Arabidopsis thaliana possesses nine genes encoding MDH isoenzymes. Activities of NAD-dependent MDHs have been detected in mitochondria, peroxisomes, cytosol and plastids. In addition, chloroplasts possess a NADP-dependent MDH isoform. The NADP-MDH as part of the 'light malate valve' plays an important role as a poising mechanism to adjust the ATP/NADPH ratio in the stroma. Its activity is strictly regulated by post-translational redox-modification mediated via the ferredoxin-thioredoxin system and fine control via the NADP<sup>+</sup> /NADP(H) ratio, thereby maintaining redox homeostasis under changing conditions. In contrast, the plastid NAD-MDH ('dark malate valve') is constitutively active and its lack leads to failure in early embryo development. While redox regulation of the main cytosolic MDH isoform has been shown, knowledge about regulation of the other two cytosolic MDHs as well as NAD-MDH isoforms from peroxisomes and mitochondria is still lacking. Knockout mutants lacking the isoforms from chloroplasts, mitochondria and peroxisomes have been characterised, but not much is known about cytosolic NAD-MDH isoforms and their role in planta. This review updates the current knowledge on MDH isoforms and the shuttle systems for intercompartmental dicarboxylate exchange, focusing on the various metabolic functions of these valves.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29933514</PMID><DateCompleted><Year>2019</Year><Month>01</Month><Day>09</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1438-8677</ISSN><JournalIssue CitedMedium="Internet"><Volume>21 Suppl 1</Volume><PubDate><Year>2019</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Plant biology (Stuttgart, Germany)</Title><ISOAbbreviation>Plant Biol (Stuttg)</ISOAbbreviation></Journal><ArticleTitle>Malate valves: old shuttles with new perspectives.</ArticleTitle><Pagination><MedlinePgn>21-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/plb.12869</ELocationID><Abstract><AbstractText>Malate valves act as powerful systems for balancing the ATP/NAD(P)H ratio required in various subcellular compartments in plant cells. As components of malate valves, isoforms of malate dehydrogenases (MDHs) and dicarboxylate translocators catalyse the reversible interconversion of malate and oxaloacetate and their transport. Depending on the co-enzyme specificity of the MDH isoforms, either NADH or NADPH can be transported indirectly. Arabidopsis thaliana possesses nine genes encoding MDH isoenzymes. Activities of NAD-dependent MDHs have been detected in mitochondria, peroxisomes, cytosol and plastids. In addition, chloroplasts possess a NADP-dependent MDH isoform. The NADP-MDH as part of the 'light malate valve' plays an important role as a poising mechanism to adjust the ATP/NADPH ratio in the stroma. Its activity is strictly regulated by post-translational redox-modification mediated via the ferredoxin-thioredoxin system and fine control via the NADP<sup>+</sup> /NADP(H) ratio, thereby maintaining redox homeostasis under changing conditions. In contrast, the plastid NAD-MDH ('dark malate valve') is constitutively active and its lack leads to failure in early embryo development. While redox regulation of the main cytosolic MDH isoform has been shown, knowledge about regulation of the other two cytosolic MDHs as well as NAD-MDH isoforms from peroxisomes and mitochondria is still lacking. Knockout mutants lacking the isoforms from chloroplasts, mitochondria and peroxisomes have been characterised, but not much is known about cytosolic NAD-MDH isoforms and their role in planta. This review updates the current knowledge on MDH isoforms and the shuttle systems for intercompartmental dicarboxylate exchange, focusing on the various metabolic functions of these valves.</AbstractText><CopyrightInformation>© 2018 The Authors. Plant Biology published by John Wiley & Sons Ltd on behalf of German Society for Plant Sciences, Royal Dutch Botanical Society.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Selinski</LastName><ForeName>J</ForeName><Initials>J</Initials><Identifier Source="ORCID">http://orcid.org/0000-0002-1247-7282</Identifier><AffiliationInfo><Affiliation>Department of Animal, Plant, and Soil Science, Australian Research Council Centre of Excellence in Plant Energy Biology, School of Life Science, La Trobe University Bundoora, Bundoora, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Scheibe</LastName><ForeName>R</ForeName><Initials>R</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-6140-6181</Identifier><AffiliationInfo><Affiliation>Division of Plant Physiology, Department of Biology/Chemistry, University of Osnabrueck, Osnabrueck, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Alexander von Humboldt-Stiftung</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>07</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant Biol (Stuttg)</MedlineTA><NlmUniqueID>101148926</NlmUniqueID><ISSNLinking>1435-8603</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008293">Malates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0U46U6E8UK</RegistryNumber><NameOfSubstance UI="D009243">NAD</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.37</RegistryNumber><NameOfSubstance UI="D008291">Malate Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.39</RegistryNumber><NameOfSubstance UI="C030574">malate dehydrogenase (decarboxylating)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019069" MajorTopicYN="N">Cell Respiration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008291" MajorTopicYN="N">Malate Dehydrogenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008293" MajorTopicYN="N">Malates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005810" MajorTopicYN="N">Multigene 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