Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.

Columbia-0 (Col-0), Wassilewskija-4 (Ws-4), and Landsberg erecta-0 (Ler-0) are used as background lines for many public Arabidopsis mutant collections, and for investigation in laboratory conditions of plant processes, including photosynthesis and response to high-intensity light (HL). The photosyst...

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Autores principales: Lan Yin, Rikard Fristedt, Andrei Herdean, Katalin Solymosi, Martine Bertrand, Mats X Andersson, Fikret Mamedov, Alexander V Vener, Benoît Schoefs, Cornelia Spetea
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Publicado: Public Library of Science (PLoS) 2012
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spelling oai:doaj.org-article:2a781f06564f465ebdaea2612b50d8b52021-11-18T08:13:44ZPhotosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.1932-620310.1371/journal.pone.0046206https://doaj.org/article/2a781f06564f465ebdaea2612b50d8b52012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23029436/?tool=EBIhttps://doaj.org/toc/1932-6203Columbia-0 (Col-0), Wassilewskija-4 (Ws-4), and Landsberg erecta-0 (Ler-0) are used as background lines for many public Arabidopsis mutant collections, and for investigation in laboratory conditions of plant processes, including photosynthesis and response to high-intensity light (HL). The photosystem II (PSII) complex is sensitive to HL and requires repair to sustain its function. PSII repair is a multistep process controlled by numerous factors, including protein phosphorylation and thylakoid membrane stacking. Here we have characterized the function and dynamics of PSII complex under growth-light and HL conditions. Ws-4 displayed 30% more thylakoid lipids per chlorophyll and 40% less chlorophyll per carotenoid than Col-0 and Ler-0. There were no large differences in thylakoid stacking, photoprotection and relative levels of photosynthetic complexes among the three accessions. An increased efficiency of PSII closure was found in Ws-4 following illumination with saturation flashes or continuous light. Phosphorylation of the PSII D1/D2 proteins was reduced by 50% in Ws-4 as compared to Col-0 and Ler-0. An increase in abundance of the responsible STN8 kinase in response to HL treatment was found in all three accessions, but Ws-4 displayed 50% lower levels than Col-0 and Ler-0. Despite this, the HL treatment caused in Ws-4 the lagest extent of PSII inactivation, disassembly, D1 protein degradation, and the largest decrease in the size of stacked thylakoids. The dilution of chlorophyll-protein complexes with additional lipids and carotenoids in Ws-4 may represent a mechanism to facilitate lateral protein traffic in the membrane, thus compensating for the lack of a full complement of STN8 kinase. Nevertheless, additional PSII damage occurs in Ws-4, which exceeds the D1 protein synthesis capacity, thus leading to enhanced photoinhibition. Our findings are valuable for selection of appropriate background line for PSII characterization in Arabidopsis mutants, and also provide the first insights into natural variation of PSII protein phosphorylation.Lan YinRikard FristedtAndrei HerdeanKatalin SolymosiMartine BertrandMats X AnderssonFikret MamedovAlexander V VenerBenoît SchoefsCornelia SpeteaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 9, p e46206 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Lan Yin
Rikard Fristedt
Andrei Herdean
Katalin Solymosi
Martine Bertrand
Mats X Andersson
Fikret Mamedov
Alexander V Vener
Benoît Schoefs
Cornelia Spetea
Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
description Columbia-0 (Col-0), Wassilewskija-4 (Ws-4), and Landsberg erecta-0 (Ler-0) are used as background lines for many public Arabidopsis mutant collections, and for investigation in laboratory conditions of plant processes, including photosynthesis and response to high-intensity light (HL). The photosystem II (PSII) complex is sensitive to HL and requires repair to sustain its function. PSII repair is a multistep process controlled by numerous factors, including protein phosphorylation and thylakoid membrane stacking. Here we have characterized the function and dynamics of PSII complex under growth-light and HL conditions. Ws-4 displayed 30% more thylakoid lipids per chlorophyll and 40% less chlorophyll per carotenoid than Col-0 and Ler-0. There were no large differences in thylakoid stacking, photoprotection and relative levels of photosynthetic complexes among the three accessions. An increased efficiency of PSII closure was found in Ws-4 following illumination with saturation flashes or continuous light. Phosphorylation of the PSII D1/D2 proteins was reduced by 50% in Ws-4 as compared to Col-0 and Ler-0. An increase in abundance of the responsible STN8 kinase in response to HL treatment was found in all three accessions, but Ws-4 displayed 50% lower levels than Col-0 and Ler-0. Despite this, the HL treatment caused in Ws-4 the lagest extent of PSII inactivation, disassembly, D1 protein degradation, and the largest decrease in the size of stacked thylakoids. The dilution of chlorophyll-protein complexes with additional lipids and carotenoids in Ws-4 may represent a mechanism to facilitate lateral protein traffic in the membrane, thus compensating for the lack of a full complement of STN8 kinase. Nevertheless, additional PSII damage occurs in Ws-4, which exceeds the D1 protein synthesis capacity, thus leading to enhanced photoinhibition. Our findings are valuable for selection of appropriate background line for PSII characterization in Arabidopsis mutants, and also provide the first insights into natural variation of PSII protein phosphorylation.
format article
author Lan Yin
Rikard Fristedt
Andrei Herdean
Katalin Solymosi
Martine Bertrand
Mats X Andersson
Fikret Mamedov
Alexander V Vener
Benoît Schoefs
Cornelia Spetea
author_facet Lan Yin
Rikard Fristedt
Andrei Herdean
Katalin Solymosi
Martine Bertrand
Mats X Andersson
Fikret Mamedov
Alexander V Vener
Benoît Schoefs
Cornelia Spetea
author_sort Lan Yin
title Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
title_short Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
title_full Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
title_fullStr Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
title_full_unstemmed Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
title_sort photosystem ii function and dynamics in three widely used arabidopsis thaliana accessions.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/2a781f06564f465ebdaea2612b50d8b5
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