ArticlePlant physiology2016
The Low Molecular Weight Protein PsaI Stabilizes the Light-Harvesting Complex II Docking Site of Photosystem I.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Complex plastome structural variation caused by intermolecular and intramolecular recombination accounts for leaf variegation inPlant diversity · 2026Article
- Structure, function, and assembly of PSI in thylakoid membranes of vascular plants.The Plant cell · 2024Review
- The plant cytosolic mPlant communications · 2023Article
- Article
- Chloroplast genome assembly ofFrontiers in plant science · 2023Article
- NADP+ supply adjusts the synthesis of photosystem I in Arabidopsis chloroplasts.Plant physiology · 2022Article
- Comparative and phylogenetic analyses of Swertia L. (Gentianaceae) medicinal plants (from Qinghai, China) based on complete chloroplast genomes.Genetics and molecular biology · 2021Article
- Composition, phosphorylation and dynamic organization of photosynthetic protein complexes in plant thylakoid membrane.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020Review
- Article
- Extensive gain and loss of photosystem I subunits in chromerid algae, photosynthetic relatives of apicomplexans.Scientific reports · 2017Article
- The plastid-encoded PsaI subunit stabilizes photosystem I during leaf senescence in tobacco.Journal of experimental botany · 2017Article
- Comparative Analysis of Light-Harvesting Antennae and State Transition in chlorina and cpSRP Mutants.Plant physiology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PsaI represents one of three low molecular weight peptides of PSI. Targeted inactivation of the plastid PsaI gene in Nicotiana tabacum has no measurable effect on photosynthetic electron transport around PSI or on accumulation of proteins involved in photosynthesis. Instead, the lack of PsaI destabilizes the association of PsaL and PsaH to PSI, both forming the light-harvesting complex (LHC)II docking site of PSI. These alterations at the LHCII binding site surprisingly did not prevent state transition but led to an increased incidence of PSI-LHCII complexes, coinciding with an elevated phosphorylation level of the LHCII under normal growth light conditions. Remarkably, LHCII was rapidly phosphorylated in ΔpsaI in darkness even after illumination with far-red light. We found that this dark phosphorylation also occurs in previously described mutants impaired in PSI function or state transition. A prompt shift of the plastoquinone (PQ) pool into a more reduced redox state in the dark caused an enhanced LHCII phosphorylation in ΔpsaI Since the redox status of the PQ pool is functionally connected to a series of physiological, biochemical, and gene expression reactions, we propose that the shift of mutant plants into state 2 in darkness represents a compensatory and/or protective metabolic mechanism. This involves an increased reduction and/or reduced oxidation of the PQ pool, presumably to sustain a balanced excitation of both photosystems upon the onset of light.
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