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Photosystem II Function and Dynamics in Three Widely Used Arabidopsis thaliana Accessions

Yin, Lan, 1979 (author)
Gothenburg University,Göteborgs universitet,Institutionen för biologi och miljövetenskap,Department of Biological and Environmental Sciences,University of Gothenburg, Sweden
Fristedt, Rikard (author)
Linköpings universitet,Cellbiologi,Hälsouniversitetet
Herdean, Andrei, 1984 (author)
Gothenburg University,Göteborgs universitet,Institutionen för biologi och miljövetenskap,Department of Biological and Environmental Sciences,University of Gothenburg, Sweden
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Solymosi, Katalin (author)
Eotvos Lorand University, Hungary
Bertrand, Martine (author)
National Institute Marine Science and Tech, France
Andersson, Mats X., 1977 (author)
Gothenburg University,Göteborgs universitet,Institutionen för biologi och miljövetenskap,Department of Biological and Environmental Sciences,University of Gothenburg, Sweden
Mamedov, Fikret (author)
Uppsala universitet,Molekylär biomimetik,fotosyntesgruppen,Uppsala University, Sweden
Vener, Alexander (author)
Linköpings universitet,Cellbiologi,Hälsouniversitetet
Schoefs, Benoit (author)
University of Maine, France
Spetea, Cornelia, 1968 (author)
Gothenburg University,Göteborgs universitet,Institutionen för biologi och miljövetenskap,Department of Biological and Environmental Sciences,University of Gothenburg, Sweden
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 (creator_code:org_t)
2012-09-28
2012
English.
In: PLoS One. - : Public Library of Science (PLoS). - 1932-6203. ; 7:9
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Subject headings

NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

Keyword

plant
photosynthesis
photosystem II
natural variation
light stress
MEDICINE

Publication and Content Type

ref (subject category)
art (subject category)

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