Natural variation in phosphorylation of photosystem II proteins in Arabidopsis thaliana: is it caused by genetic variation in the STN kinases?

P.J. Flood, L. Yin, A. Herdean, J. Harbinson, M.G.M. Aarts, C. Spetea

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5 Citations (Scopus)

Abstract

Reversible phosphorylation of photosystem II (PSII) proteins is an important regulatory mechanism that can protect plants from changes in ambient light intensity and quality. We hypothesized that there is natural variation in this process in Arabidopsis (Arabidopsis thaliana), and that this results from genetic variation in the STN7 and STN8 kinase genes. To test this, Arabidopsis accessions of diverse geographical origins were exposed to two light regimes, and the levels of phospho-D1 and phospho-light harvesting complex II (LHCII) proteins were quantified by western blotting with anti-phosphothreonine antibodies. Accessions were classified as having high, moderate or low phosphorylation relative to Col-0. This variation could not be explained by the abundance of the substrates in thylakoid membranes. In genotypes with atrazine-resistant forms of the D1 protein, low D1 and LHCII protein phosphorylation was observed, which may be due to low PSII efficiency, resulting in reduced activation of the STN kinases. In the remaining genotypes, phospho-D1 levels correlated with STN8 protein abundance in high-light conditions. In growth light, D1 and LHCII phosphorylation correlated with longitude and in the case of LHCII phosphorylation also with temperature variability. This suggests a possible role of natural variation in PSII protein phosphorylation in the adaptation of Arabidopsis to diverse environments
Original languageEnglish
Article number20130499
Number of pages9
JournalPhilosophical Transactions of the Royal Society B. Biological sciences
Volume369
Issue number1640
DOIs
Publication statusPublished - 2014

Keywords

  • harvesting complex ii
  • cyclic electron flow
  • photosynthetic acclimation
  • state transitions
  • plant photosynthesis
  • substrate level
  • core proteins
  • chlorophyll-a
  • in-vivo
  • light

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