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Antenna complexes protect Photosystem I from Photoinhibition

BACKGROUND: 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 f...

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Autores principales: Alboresi, Alessandro, Ballottari, Matteo, Hienerwadel, Rainer, Giacometti, Giorgio M, Morosinotto, Tomas
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2704212/
https://www.ncbi.nlm.nih.gov/pubmed/19508723
http://dx.doi.org/10.1186/1471-2229-9-71
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author Alboresi, Alessandro
Ballottari, Matteo
Hienerwadel, Rainer
Giacometti, Giorgio M
Morosinotto, Tomas
author_facet Alboresi, Alessandro
Ballottari, Matteo
Hienerwadel, Rainer
Giacometti, Giorgio M
Morosinotto, Tomas
author_sort Alboresi, Alessandro
collection PubMed
description BACKGROUND: 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. RESULTS: 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. CONCLUSION: 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.
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spelling pubmed-27042122009-07-01 Antenna complexes protect Photosystem I from Photoinhibition Alboresi, Alessandro Ballottari, Matteo Hienerwadel, Rainer Giacometti, Giorgio M Morosinotto, Tomas BMC Plant Biol Research Article BACKGROUND: 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. RESULTS: 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. CONCLUSION: 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. BioMed Central 2009-06-09 /pmc/articles/PMC2704212/ /pubmed/19508723 http://dx.doi.org/10.1186/1471-2229-9-71 Text en Copyright © 2009 Alboresi et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Alboresi, Alessandro
Ballottari, Matteo
Hienerwadel, Rainer
Giacometti, Giorgio M
Morosinotto, Tomas
Antenna complexes protect Photosystem I from Photoinhibition
title Antenna complexes protect Photosystem I from Photoinhibition
title_full Antenna complexes protect Photosystem I from Photoinhibition
title_fullStr Antenna complexes protect Photosystem I from Photoinhibition
title_full_unstemmed Antenna complexes protect Photosystem I from Photoinhibition
title_short Antenna complexes protect Photosystem I from Photoinhibition
title_sort antenna complexes protect photosystem i from photoinhibition
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2704212/
https://www.ncbi.nlm.nih.gov/pubmed/19508723
http://dx.doi.org/10.1186/1471-2229-9-71
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