Reversible phosphorylation of photosystem II light harvesting complexes (LHCII) is a well-established protective mechanism enabling efficient response to changing light conditions. However, changes in LHCII phosphorylation were also observed in response to abiotic stress regardless of photoperiod. This study aimed to investigate the impact of dark-chilling on LHCII phosphorylation pattern in chilling-tolerant and to check whether the disturbed LHCII phosphorylation process will impact the response of Arabidopsis to the dark-chilling conditions. We analyzed the pattern of LHCII phosphorylation, the organization of chlorophyll-protein complexes, and the level of chilling tolerance by combining biochemical and spectroscopy techniques under dark-chilling and dark conditions in Arabidopsis mutants with disrupted LHCII phosphorylation. Our results show that during dark-chilling, LHCII phosphorylation decreased in all examined plant lines and that no significant differences in dark-chilling response were registered in tested lines. Interestingly, after 24 h of darkness, a high increase in LHCII phosphorylation was observed, co-occurring with a significant F/F parameter decrease. The highest drop of F/F was detected in the line-mutant, where the LHCII is not phosphorylated, due to the lack of STN7 kinase. Our results imply that STN7 kinase activity is important for mitigating the adverse effects of prolonged darkness.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9100030 | PMC |
http://dx.doi.org/10.3390/ijms23094531 | DOI Listing |
Commun Biol
August 2024
Hubei Provincial Key Laboratory for Protection and Application of Special Plant Germplasm in Wuling Area of China, College of Life Sciences, South-Central Minzu University, Wuhan, China.
Chrysosplenium sinicum, a traditional Tibetan medicinal plant, can successfully thrive in low-light environments for long periods of time. To investigate the adaptive evolution of shade plants in low-light environments, we generated a chromosome-scale genome assembly (~320 Mb) for C. sinicum by combining PacBio sequencing and Hi-C technologies.
View Article and Find Full Text PDFPlant Cell
October 2024
Aix Marseille Univ, CEA, CNRS, BIAM, Photosynthesis and Environment, F-13115 Saint Paul-Lez-Durance, France.
In oxygenic photosynthesis, state transitions distribute light energy between PSI and PSII. This regulation involves reduction of the plastoquinone pool, activation of the state transitions 7 (STT7) protein kinase by the cytochrome (cyt) b6f complex, and phosphorylation and migration of light harvesting complexes II (LHCII). In this study, we show that in Chlamydomonas reinhardtii, the C-terminus of the cyt b6 subunit PetB acts on phosphorylation of STT7 and state transitions.
View Article and Find Full Text PDFBMC Plant Biol
June 2024
Department of Metabolic Regulation, Institute of Biochemistry, Faculty of Biology, University of Warsaw, Miecznikowa 1, Warsaw, 02-096, Poland.
Nat Plants
March 2024
Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
The balance between linear electron transport (LET) and cyclic electron transport (CET) plays an essential role in plant adaptation and protection against photo-induced damage. This balance is largely maintained by phosphorylation-driven alterations in the PSII-LHCII assembly and thylakoid membrane stacking. During the dark-to-light transition, plants shift this balance from CET, which prevails to prevent overreduction of the electron transport chain and consequent photo-induced damage, towards LET, which enables efficient CO assimilation and biomass production.
View Article and Find Full Text PDFNew Phytol
April 2024
Faculty of Biology, Technion, Haifa, 32000, Israel.
The phosphorylation of photosystem II (PSII) and its antenna (LHCII) proteins has been studied, and its involvement in state transitions and PSII repair is known. Yet, little is known about the phosphorylation of photosystem I (PSI) and its antenna (LHCI) proteins. Here, we applied proteomics analysis to generate a map of the phosphorylation sites of the PSI-LHCI proteins in Chlorella ohadii cells that were grown under low or extreme high-light intensities (LL and HL).
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!