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• W2807002246 abstract "Discovery of rapidly turning-over photosynthetic complex protein subunits has revealed potential photodamage targets and highlighted new points of control to maintain photosystem homeostasis under optimal and stress conditions. ZEP, PGRL1, and NDH complex-dependent cyclic electron flow can act as photoprotection pathways in response to light stresses. Photosynthetic protein phosphorylation in state transition may act in protein stability control. Rapid protein synthesis and degradation pathway in different cellular compartments could combine to ensure photoprotection in plants. Rapid protein degradation and replacement is an important response to photodamage and a means of photoprotection by recovering proteostasis. Protein turnover and translation efficiency studies have discovered fast turnover subunits in cytochrome b6f and the NAD(P)H dehydrogenase (NDH) complex, in addition to PSII subunit D1. Mutations of these complexes have been linked to enhanced photodamage at least partially via cyclic electron flow. Photodamage and photoprotection involving cytochrome b6f, NDH complex, cyclic electron flow, PSI, and nonphotochemical quenching proteins have been reported. Here, we propose that the rapid turnover of specific proteins in cytochrome b6f and the NDH complex need to be characterised and compared with the inhibition of PSII by excess excitation energy and PSI by excess electron flux to expand our understanding of photoinhibition mechanisms. Rapid protein degradation and replacement is an important response to photodamage and a means of photoprotection by recovering proteostasis. Protein turnover and translation efficiency studies have discovered fast turnover subunits in cytochrome b6f and the NAD(P)H dehydrogenase (NDH) complex, in addition to PSII subunit D1. Mutations of these complexes have been linked to enhanced photodamage at least partially via cyclic electron flow. Photodamage and photoprotection involving cytochrome b6f, NDH complex, cyclic electron flow, PSI, and nonphotochemical quenching proteins have been reported. Here, we propose that the rapid turnover of specific proteins in cytochrome b6f and the NDH complex need to be characterised and compared with the inhibition of PSII by excess excitation energy and PSI by excess electron flux to expand our understanding of photoinhibition mechanisms. used here to describe modifications to protein properties that contribute to the decrease in photosynthesis efficiency through the actions of light. High irradiance, fluctuating light, and short wavelength light can each cause different levels or types of damage to photosynthetic proteins, leading to a reduction in photosynthesis efficiency. Plants are equipped with different photoprotection mechanisms to limit photodamage and overcome its effects on photosynthetic rate. the combination of degradation and synthesis of specific proteins that maintains the steady-state abundance of each protein in a cell. It maintains protein quality and function throughout different stages of growth and development. It is a high energy cost to cells, representing at least 25% of all cellular ATP use." @default.
• W2807002246 created "2018-06-13" @default.
• W2807002246 creator A5004433673 @default.
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• W2807002246 date "2018-08-01" @default.
• W2807002246 modified "2023-10-11" @default.
• W2807002246 title "Mechanisms of Photodamage and Protein Turnover in Photoinhibition" @default.
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• W2807002246 doi "https://doi.org/10.1016/j.tplants.2018.05.004" @default.
• W2807002246 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29887276" @default.
• W2807002246 hasPublicationYear "2018" @default.
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