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  Stromal NADH supplied by PHOSPHOGLYCERATE DEHYDROGENASE3 is crucial for photosynthetic performance

Höhner, R., Day, P. M., Zimmermann, S. E., Lopez, L. S., Krämer, M., Giavalisco, P., et al. (2021). Stromal NADH supplied by PHOSPHOGLYCERATE DEHYDROGENASE3 is crucial for photosynthetic performance. Plant Physiology, 186(1), 142-167. doi:10.1093/plphys/kiaa117.

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 Creators:
Höhner, Ricarda1, Author
Day, Philip M1, Author
Zimmermann, Sandra E1, Author
Lopez, Laura S1, Author
Krämer, Moritz1, Author
Giavalisco, Patrick1, Author
Correa Galvis, V.2, Author              
Armbruster, U.2, Author              
Schöttler, M. A.3, Author              
Jahns, Peter1, Author
Krüger, Stephan1, Author
Kunz, Hans-Henning1, Author
Affiliations:
1external, ou_persistent22              
2Regulation of Photosynthesis, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_2205653              
3Photosynthesis Research, Department Bock, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753323              

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 Abstract: During photosynthesis, electrons travel from light-excited chlorophyll molecules along the electron transport chain to the final electron acceptor 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 diverted from NADPH via the CBBC into the separate NADH redox pool. pgdh3 loss-of-function mutants revealed an over-reduced 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 non-photochemical 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 aid 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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Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1093/plphys/kiaa117
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Title: Plant Physiology
  Other : Plant Physiol.
Source Genre: Journal
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Publ. Info: Bethesda, Md. : American Society of Plant Biologists
Pages: - Volume / Issue: 186 (1) Sequence Number: - Start / End Page: 142 - 167 Identifier: ISSN: 0032-0889
CoNE: https://pure.mpg.de/cone/journals/resource/991042744294438