
In addition to linear electron transport, photosystem I cyclic electron transport (PSI-CET) contributes to photosynthesis and photoprotection. In Arabidopsis (Arabidopsis thaliana), PSI-CET consists of two partially redundant pathways, one of which is the PROTON GRADIENT REGULATION5 (PGR5)/PGR5-LIKE PHOTOSYNTHETIC PHENOTYPE1 (PGRL1)-dependent pathway. Although the physiological significance of PSI-CET is widely recognized, the regulatory mechanism behind these pathways remains largely unknown. Here, we report on the regulation of the PGR5/PGRL1-dependent pathway by the m-type thioredoxins (Trx m). Genetic and phenotypic characterizations of multiple mutants indicated the physiological interaction between Trx m and the PGR5/PGRL1-dependent pathway in vivo. Using purified Trx proteins and ruptured chloroplasts, in vitro, we showed that the reduced form of Trx m specifically decreased the PGR5/PGRL1-dependent plastoquinone reduction. In planta, Trx m4 directly interacted with PGRL1 via disulfide complex formation. Analysis of the transgenic plants expressing PGRL1 Cys variants demonstrated that Cys-123 of PGRL1 is required for Trx m4-PGRL1 complex formation. Furthermore, the Trx m4-PGRL1 complex was transiently dissociated during the induction of photosynthesis. We propose that Trx m directly regulates the PGR5/PGRL1-dependent pathway by complex formation with PGRL1.
Chloroplasts, Photosystem I Protein Complex, Arabidopsis Proteins, Plastoquinone, Photosynthetic Reaction Center Complex Proteins, Arabidopsis, Membrane Proteins, Plants, Genetically Modified, Electron Transport, Chloroplast Thioredoxins, Disulfides, Photosynthesis
Chloroplasts, Photosystem I Protein Complex, Arabidopsis Proteins, Plastoquinone, Photosynthetic Reaction Center Complex Proteins, Arabidopsis, Membrane Proteins, Plants, Genetically Modified, Electron Transport, Chloroplast Thioredoxins, Disulfides, Photosynthesis
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