Universität zu Köln

Hohner, Ricarda, Day, Philip M., Zimmermann, Sandra E., Lopez, Laura S., Kramer, Moritz, Giavalisco, Patrick, Galvis, Viviana Correa, Armbruster, Ute, Schoettler, Mark Aurel, Jahns, Peter, Krueger, Stephan and Kunz, Hans-Henning (2021). Stromal NADH supplied by PHOSPHOGLYCERATE DEHYDROGENASE3 is crucial for photosynthetic performance. Plant Physiol., 186 (1). S. 142 - 168. CARY: OXFORD UNIV PRESS INC. ISSN 1532-2548

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Abstract

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 C-3-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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Hohner, Ricarda UNSPECIFIED UNSPECIFIED UNSPECIFIED Day, Philip M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Zimmermann, Sandra E. UNSPECIFIED UNSPECIFIED UNSPECIFIED Lopez, Laura S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Kramer, Moritz UNSPECIFIED UNSPECIFIED UNSPECIFIED Giavalisco, Patrick UNSPECIFIED UNSPECIFIED UNSPECIFIED Galvis, Viviana Correa UNSPECIFIED UNSPECIFIED UNSPECIFIED Armbruster, Ute UNSPECIFIED UNSPECIFIED UNSPECIFIED Schoettler, Mark Aurel UNSPECIFIED UNSPECIFIED UNSPECIFIED Jahns, Peter UNSPECIFIED UNSPECIFIED UNSPECIFIED Krueger, Stephan UNSPECIFIED UNSPECIFIED UNSPECIFIED Kunz, Hans-Henning UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-591861
DOI:	10.1093/plphys/kiaa117
Journal or Publication Title:	Plant Physiol.
Volume:	186
Number:	1
Page Range:	S. 142 - 168
Date:	2021
Publisher:	OXFORD UNIV PRESS INC
Place of Publication:	CARY
ISSN:	1532-2548
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language DEPENDENT MALATE-DEHYDROGENASE; PROTON MOTIVE FORCE; TRIOSE-PHOSPHATE/PHOSPHATE TRANSLOCATOR; AMINO-ACID; THYLAKOID MEMBRANE; ELECTRON-TRANSPORT; PHOTOSYSTEM-I; 3-PHOSPHOGLYCERATE DEHYDROGENASE; SERINE BIOSYNTHESIS; COFACTOR PREFERENCE Multiple languages Plant Sciences Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/59186