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Protein–Protein Interactions Induce pH-Dependent and Zeaxanthin-Independent Photoprotection in the Plant Light-Harvesting Complex, LHCII
Name
Sonetal2021JacsmultipleLHCIInanodisks.pdf
Description
Accepted version
Size
7.2 MB
Format
Adobe PDF
Checksum (MD5)
ce5670e6e8c0456638ecb46dfff80677
Author(s)
Son, Minjung
Moya, Raymundo
Pinnola, Alberta
Bassi, Roberto
Schlau-Cohen, Gabriela S
Date Issued
October 27, 2021
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Son, Minjung, Moya, Raymundo, Pinnola, Alberta, Bassi, Roberto and Schlau-Cohen, Gabriela S. 2021. "Protein–Protein Interactions Induce pH-Dependent and Zeaxanthin-Independent Photoprotection in the Plant Light-Harvesting Complex, LHCII." Journal of the American Chemical Society, 143 (42).
Version
Author's final manuscript
Abstract
Plants use energy from the sun yet also require protection against the generation of deleterious photoproducts from excess energy. Photoprotection in green plants, known as nonphotochemical quenching (NPQ), involves thermal dissipation of energy and is activated by a series of interrelated factors: a pH drop in the lumen, accumulation of the carotenoid zeaxanthin (Zea), and formation of arrays of pigment-containing antenna complexes. However, understanding their individual contributions and their interactions has been challenging, particularly for the antenna arrays, which are difficult to manipulate in vitro. Here, we achieved systematic and discrete control over the array size for the principal antenna complex, light-harvesting complex II, using near-native in vitro membranes called nanodiscs. Each of the factors had a distinct influence on the level of dissipation, which was characterized by measurements of fluorescence quenching and ultrafast chlorophyll-to-carotenoid energy transfer. First, an increase in array size led to a corresponding increase in dissipation; the dramatic changes in the chlorophyll dynamics suggested that this is due to an allosteric conformational change of the protein. Second, a pH drop increased dissipation but exclusively in the presence of protein-protein interactions. Third, no Zea dependence was identified which suggested that Zea regulates a distinct aspect of NPQ. Collectively, these results indicate that each factor provides a separate type of control knob for photoprotection, which likely enables a flexible and tunable response to solar fluctuations.
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Creative Commons Attribution-Noncommercial-Share Alike
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DOI of Published Version
10.1021/jacs.1c07385
