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- W4386475235 abstract "Abstract The thylakoid protein Proton Gradient Regulation5 (PGR5) is thought to be a key component of cyclic electron flux around photosystem I. The pgr5 mutant is characterized by impaired proton motive force (pmf) formation across the thylakoid membrane, decreased photoprotective non-photochemical quenching (NPQ), and an over-reduction of the PSI acceptor side. This over-reduction has been attributed to impaired photosynthetic control, which down-regulates plastoquinol re-oxidation at the cytochrome b 6 f complex when the lumen is strongly acidified. Here, using the cgl160 ATP synthase assembly mutant, we show that in cgl160 pgr5 double mutants, both the pmf across the thylakoid membrane and NPQ are fully restored to wild-type levels. However, the acceptor-side limitation of PSI in the double mutants stays comparable to the single pgr5 mutant. This demonstrates that impaired photosynthetic control is not causal for the over-reduction of the PSI acceptor side in pgr5 . Instead, we show that both in pgr5 and the clg160 pgr5 mutants, the entire high-potential chain from cytochrome f to PSI remains strongly reduced in high light. This leads to insufficient oxidizing power for plastoquinol re-oxidation by the cytochrome b 6 f complex, thus impairing pmf formation. We conclude that PGR5 plays a critical role in electron partitioning downstream of PSI." @default.
- W4386475235 created "2023-09-07" @default.
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- W4386475235 date "2023-09-06" @default.
- W4386475235 modified "2023-09-27" @default.
- W4386475235 title "A congestion downstream of PSI causes the over-reduction of the electron transport chain in pgr5 independent of membrane energization" @default.
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- W4386475235 doi "https://doi.org/10.1101/2023.09.01.555968" @default.
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