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• W2108015510 abstract "Photosystems are composed of two moieties, a reaction center and a peripheral antenna system. In photosynthetic eukaryotes the latter system is composed of proteins belonging to Lhc family. An increasing set of evidences demonstrated how these polypeptides play a relevant physiological function in both light harvesting and photoprotection. Despite the sequence similarity between antenna proteins associated with the two Photosystems, present knowledge on their physiological role is mostly limited to complexes associated to Photosystem II.In this work we analyzed the physiological role of Photosystem I antenna system in Arabidopsis thaliana both in vivo and in vitro. Plants depleted in individual antenna polypeptides showed a reduced capacity for photoprotection and an increased production of reactive oxygen species upon high light exposure. In vitro experiments on isolated complexes confirmed that depletion of antenna proteins reduced the resistance of isolated Photosystem I particles to high light and that the antenna is effective in photoprotection only upon the interaction with the core complex.We show that antenna proteins play a dual role in Arabidopsis thaliana Photosystem I photoprotection: first, a Photosystem I with an intact antenna system is more resistant to high light because of a reduced production of reactive oxygen species and, second, antenna chlorophyll-proteins are the first target of high light damages. When photoprotection mechanisms become insufficient, the antenna chlorophyll proteins act as fuses: LHCI chlorophylls are degraded while the reaction center photochemical activity is maintained. Differences with respect to photoprotection strategy in Photosystem II, where the reaction center is the first target of photoinhibition, are discussed." @default.
• W2108015510 created "2016-06-24" @default.
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• W2108015510 date "2009-06-09" @default.
• W2108015510 modified "2023-10-09" @default.
• W2108015510 title "Antenna complexes protect Photosystem I from Photoinhibition" @default.
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• W2108015510 doi "https://doi.org/10.1186/1471-2229-9-71" @default.
• W2108015510 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2704212" @default.
• W2108015510 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19508723" @default.
• W2108015510 hasPublicationYear "2009" @default.
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