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

Yin, L; Fristedt, R; Herdean, A; Solymosi, K; Bertrand, M; Andersson, MX; Mamedov, F; Vener, AV; Schoefs, B; Spetea, C

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

Yin, L Fristedt, R Herdean, A

Solymosi, K Bertrand, M Andersson, MX Mamedov, F Vener, AV Schoefs, B Spetea, C

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Publisher:: PUBLIC LIBRARY SCIENCE
Publication Type:: Journal Article
Citation:: PloS one, 2012, 7, (9), pp. e46206
Issue Date:: 2012-01

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Field	Value	Language
dc.contributor.author	Yin, L
dc.contributor.author	Fristedt, R
dc.contributor.author	Herdean, A https://orcid.org/0000-0003-2143-0213
dc.contributor.author	Solymosi, K
dc.contributor.author	Bertrand, M
dc.contributor.author	Andersson, MX
dc.contributor.author	Mamedov, F
dc.contributor.author	Vener, AV
dc.contributor.author	Schoefs, B
dc.contributor.author	Spetea, C
dc.date.accessioned	2020-09-04T00:28:17Z
dc.date.available	2012-08-30
dc.date.available	2020-09-04T00:28:17Z
dc.date.issued	2012-01
dc.identifier.citation	PloS one, 2012, 7, (9), pp. e46206
dc.identifier.issn	1932-6203
dc.identifier.issn	1932-6203
dc.identifier.uri	http://hdl.handle.net/10453/142540
dc.description.abstract	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.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	PUBLIC LIBRARY SCIENCE
dc.relation.ispartof	PloS one
dc.relation.isbasedon	10.1371/journal.pone.0046206
dc.rights	info:eu-repo/semantics/openAccess
dc.subject.classification	General Science & Technology
dc.subject.mesh	Cell Membrane
dc.subject.mesh	Thylakoids
dc.subject.mesh	Arabidopsis
dc.subject.mesh	Chlorophyll
dc.subject.mesh	Photosystem II Protein Complex
dc.subject.mesh	Protein Kinases
dc.subject.mesh	Lipids
dc.subject.mesh	Arabidopsis Proteins
dc.subject.mesh	Species Specificity
dc.subject.mesh	Photosynthesis
dc.subject.mesh	Protein Transport
dc.subject.mesh	Phosphorylation
dc.subject.mesh	Mutation
dc.subject.mesh	Light
dc.subject.mesh	Photoperiod
dc.subject.mesh	Arabidopsis
dc.subject.mesh	Arabidopsis Proteins
dc.subject.mesh	Cell Membrane
dc.subject.mesh	Chlorophyll
dc.subject.mesh	Light
dc.subject.mesh	Lipids
dc.subject.mesh	Mutation
dc.subject.mesh	Phosphorylation
dc.subject.mesh	Photoperiod
dc.subject.mesh	Photosynthesis
dc.subject.mesh	Photosystem II Protein Complex
dc.subject.mesh	Protein Kinases
dc.subject.mesh	Protein Transport
dc.subject.mesh	Species Specificity
dc.subject.mesh	Thylakoids
dc.title	Photosystem II function and dynamics in three widely used Arabidopsis thaliana accessions.
dc.type	Journal Article
utslib.citation.volume	7
utslib.location.activity	United States
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - C3 - Climate Change Cluster
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	open_access	*
dc.date.updated	2020-09-04T00:28:04Z
pubs.issue	9
pubs.publication-status	Published
pubs.volume	7
utslib.citation.issue	9

Abstract:

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.

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http://hdl.handle.net/10453/142540