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Tethering ferredoxin-NADP + reductase to photosystem I promotes photosynthetic cyclic electron transfer
Open accessPreprint — published as 10.1093/plcell/koaf042
Abstract
Fixing CO 2 via photosynthesis requires ATP and NADPH. Linear electron transfer (LET) supplies both metabolites, yet depending on environmental conditions, additional ATP is required which can be generated by cyclic electron transfer (CET). How the balance between LET and CET is set remains largely unknown. Ferredoxin(FD)-NADP + reductase (FNR) has been suggested to act as the switch, channelling photosynthetic electrons to LET when it is bound to photosystem I (PSI) or CET when bound to cytochrome b 6 f . The essential role of FNR in LET precludes the use of a direct gene knock-out to test this hypothesis. We circumvented this problem by using CRISPR-Cas9 gene editing in Chlamydomonas reinhardtii to create a chimeric form of FNR tethered to PSI via PSAF. Chimeric FNR mutants exhibited impaired photosynthetic growth relative to the wild type, and decreased LET and non-photochemical quenching (NPQ) under high CO 2 conditions. However, higher rates of CET and increased NPQ were found in the mutants under low CO 2 or low O 2 conditions where CET is normally up-regulated. Thus, rather than PSI-FNR interactions promoting LET, tethering FNR to PSI promotes CET at the expense of LET and CO 2 fixation.
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Global quantification of mammalian gene expression control
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Metadata
- Authors
- Emrich-Mills, T. Z., Proctor, M. S., Degen, G. E., Jackson, P. J., Richardson, K. H., Hawkings, F. R., Buchert, F., Hitchcock, A., Hunter, C. N., Mackinder, L. C. M., Hippler, M., & Johnson, M. P.
- Affiliations
- University of Sheffield (GB)
- Diamond Light Source (GB)
- University of Münster (DE)
- University of York (GB)
- Okayama University (JP)
- Corresponding author
- Johnson, Matthew P.
- ORCID
- Venue
- The Plant Cell
- Publisher
- openRxiv
- Published
- 2024-11-03
- Volume
- 37
- Issue
- 3
- ISSN
- 1040-4651 (ISSN-L)
- PMC
- PMC11912148
- OpenAlex
- W4408129006
- Cited by
- 19
- References
- 1
- Citations by year
- 2026: 15 · 2025: 4
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The Plant Cell (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- Funders
- Leverhulme Trust (RPG-2021-345, RPG-2019-045)
- Deutsche Forschungsgemeinschaft (HI 739/13-3, DFG FOR 5573)
- Biotechnology and Biological Sciences Research Council (BB/W015269/1, BB/V006630/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Keywords
- ferredoxin-NADP+ reductase, photosystem I, cyclic electron flow, NADPH production, non-photochemical quenching, proton gradient, CO2 fixation, Chlamydomonas reinhardtii, CRISPR/Cas9 genome editing
- MeSH terms
- Electron Transport, Ferredoxin-NADP Reductase, NADP, Photosynthesis, Chlamydomonas reinhardtii, Photosystem I Protein Complex, CRISPR-Cas Systems
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