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Stromal NADH supplied by PHOSPHOGLYCERATE DEHYDROGENASE3 is crucial for photosynthetic performance.
Höhner, Ricarda; Day, Philip M; Zimmermann, Sandra E; Lopez, Laura S; Krämer, Moritz; Giavalisco, Patrick; Correa Galvis, Viviana; Armbruster, Ute; Schöttler, Mark Aurel; Jahns, Peter; Krueger, Stephan; Kunz, Hans-Henning.
Afiliación
  • Höhner R; School of Biological Sciences, Washington State University, Pullman, WA 99164-4236, USA.
  • Day PM; School of Biological Sciences, Washington State University, Pullman, WA 99164-4236, USA.
  • Zimmermann SE; Biocenter University of Cologne, Institute for Plant Science, Cologne 50674, Germany.
  • Lopez LS; School of Biological Sciences, Washington State University, Pullman, WA 99164-4236, USA.
  • Krämer M; School of Biological Sciences, Washington State University, Pullman, WA 99164-4236, USA.
  • Giavalisco P; Max Planck Institute for Biology of Ageing, Cologne 50933, Germany.
  • Correa Galvis V; Max Planck Institute of Molecular Plant Physiology, Wissenschaftspark Golm, Potsdam 14476, Germany.
  • Armbruster U; Max Planck Institute of Molecular Plant Physiology, Wissenschaftspark Golm, Potsdam 14476, Germany.
  • Schöttler MA; Max Planck Institute of Molecular Plant Physiology, Wissenschaftspark Golm, Potsdam 14476, Germany.
  • Jahns P; Plant Biochemistry, Heinrich-Heine-University Düsseldorf, Düsseldorf D-40225, Germany.
  • Krueger S; Biocenter University of Cologne, Institute for Plant Science, Cologne 50674, Germany.
  • Kunz HH; School of Biological Sciences, Washington State University, Pullman, WA 99164-4236, USA.
Plant Physiol ; 186(1): 142-167, 2021 05 27.
Article en En | MEDLINE | ID: mdl-33779763
During photosynthesis, electrons travel from light-excited chlorophyll molecules along the electron transport chain to the final electron acceptor nicotinamide adenine dinucleotide phosphate (NADP) to form NADPH, which fuels the Calvin-Benson-Bassham cycle (CBBC). To allow photosynthetic reactions to occur flawlessly, a constant resupply of the acceptor NADP is mandatory. Several known stromal mechanisms aid in balancing the redox poise, but none of them utilizes the structurally highly similar coenzyme NAD(H). Using Arabidopsis (Arabidopsis thaliana) as a C3-model, we describe a pathway that employs the stromal enzyme PHOSPHOGLYCERATE DEHYDROGENASE 3 (PGDH3). We showed that PGDH3 exerts high NAD(H)-specificity and is active in photosynthesizing chloroplasts. PGDH3 withdrew its substrate 3-PGA directly from the CBBC. As a result, electrons become diverted from NADPH via the CBBC into the separate NADH redox pool. pgdh3 loss-of-function mutants revealed an overreduced NADP(H) redox pool but a more oxidized plastid NAD(H) pool compared to wild-type plants. As a result, photosystem I acceptor side limitation increased in pgdh3. Furthermore, pgdh3 plants displayed delayed CBBC activation, changes in nonphotochemical quenching, and altered proton motive force partitioning. Our fluctuating light-stress phenotyping data showed progressing photosystem II damage in pgdh3 mutants, emphasizing the significance of PGDH3 for plant performance under natural light environments. In summary, this study reveals an NAD(H)-specific mechanism in the stroma that aids in balancing the chloroplast redox poise. Consequently, the stromal NAD(H) pool may provide a promising target to manipulate plant photosynthesis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fotosíntesis / Arabidopsis / Proteínas de Arabidopsis / Fosfoglicerato-Deshidrogenasa / NAD Idioma: En Revista: Plant Physiol Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fotosíntesis / Arabidopsis / Proteínas de Arabidopsis / Fosfoglicerato-Deshidrogenasa / NAD Idioma: En Revista: Plant Physiol Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos