The light-driven water-splitting reaction of photosystem II exposes its key reaction center core protein subunits to irreversible oxidative photodamage. A rapid repair cycle replaces the photodamaged core subunits in plants, but how the large antenna-core supercomplex structures of plant photosystem II disassemble for repair is not currently understood. Here, we report the specific involvement of phosphorylation in removal of the peripheral antenna from the core and monomerization of the dimeric cores. However, monomeric cores disassemble further into smaller subcomplexes, even in the absence of phosphorylation, suggesting that there are other unknown mechanisms of disassembly. In this regard, we show that oxidative modifications of amino acids in core protein subunits of photosystem II are active mediators of monomeric core disassembly. Oxidative modifications thus likely disassemble only the damaged monomeric cores, ensuring an economical photosystem disassembly process. Taken together, our results suggest that phosphorylation and oxidative modification play distinct roles in photosystem II disassembly and repair.
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http://dx.doi.org/10.1016/j.xplc.2024.101202 | DOI Listing |
Plant Commun
December 2024
Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN 47907, USA. Electronic address:
The light-driven water-splitting reaction of photosystem II exposes its key reaction center core protein subunits to irreversible oxidative photodamage. A rapid repair cycle replaces the photodamaged core subunits in plants, but how the large antenna-core supercomplex structures of plant photosystem II disassemble for repair is not currently understood. Here, we report the specific involvement of phosphorylation in removal of the peripheral antenna from the core and monomerization of the dimeric cores.
View Article and Find Full Text PDFPlant Cell Physiol
December 2024
Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Krakow 30-387, Poland.
The synthesis and assembly of functioning photosynthetic complexes in chloroplasts developing from etioplasts during the de-etiolation of angiosperm seedlings are imperative for the plant's autotrophic lifestyle. This study compared the de-etiolation process under monochromatic red or blue light of equal photon flux density during a 24-h illumination period of etiolated Arabidopsis seedlings. The aim was to elucidate the impact of these light wavelengths on the etioplast-to-chloroplast transformation and the initiation of light-dependent photosynthetic reactions.
View Article and Find Full Text PDFNat Commun
June 2024
Key Laboratory of Biomacromolecules (CAS), National Laboratory of Biomacromolecules, CAS Centre for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Photosystem II (PSII) catalyzes water oxidation and plastoquinone reduction by utilizing light energy. It is highly susceptible to photodamage under high-light conditions and the damaged PSII needs to be restored through a process known as the PSII repair cycle. The detailed molecular mechanism underlying the PSII repair process remains mostly elusive.
View Article and Find Full Text PDFPhysiol Plant
November 2023
Molecular Plant Biology, University of Turku, Turku, Finland.
Disassembly and degradation of the photosynthetic protein complexes during autumn senescence, a vital step to ensure efficient nutrient relocalization for winter storage, is poorly understood. Concomitantly with the degradation, anthocyanins are often synthesized. However, as to why leaves accumulate red pigments, no consensus exists.
View Article and Find Full Text PDFJ Exp Bot
January 2024
Department of Biotechnology, Faculty of Science, Palacký University Olomouc, Olomouc, Czech Republic.
The photosynthesis-induced accumulation of reactive oxygen species in chloroplasts can lead to oxidative stress, triggering changes in protein synthesis, degradation, and the assembly/disassembly of protein complexes. Using shot-gun proteomics, we identified methyl viologen-induced changes in protein abundance in wild-type Arabidopsis and oxidative stress-hypersensitive fsd1-1 and fsd1-2 knockout mutants, which are deficient in IRON SUPEROXIDE DISMUTASE 1 (FSD1). The levels of proteins that are localized in chloroplasts and the cytoplasm were modified in all lines treated with methyl viologen.
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