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Lead induced changes in phosphorylation of PSII proteins in low light grown pea plants

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Abstract

Light-intensity and redox-state induced thylakoid proteins phosphorylation involved in structural changes and in regulation of protein turnover. The presence of heavy metal ions triggers a wide range of cellular responses including changes in plant growth and photosynthesis. Plants have evolved a number of mechanisms to protect photosynthetic apparatus. We have characterized the effect of lead on PSII protein phosphorylation in pea (Pisum sativum L.) plants grown in low light conditions. Pb ions affected only slightly photochemical efficiency of PSII and had no effect on organization of thylakoid complexes. Lead activated strongly phosphorylation of PSII core D1 protein and dephosphorylation of this protein did not proceed in far red light. D1 protein was also not degraded in this conditions. However, phosphorylation of LHCII proteins was not affected by lead. These results indicate that Pb2+ stimulate the phosphorylation of PSII core proteins and by disturbing the disassembly of supercomplexes play a role in PSII repair mechanism. LHCII phosphorylation could control the distribution of energy between the photosystems in low light conditions. This demonstrates that plants may respond to heavy metals by induction different pathways responsible for protein protection under stress conditions.

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Acknowledgments

These studies were founded by the grant NN 303 811740 from the Ministry of Science and High Education of Poland and by State Committee for Scientific Research, through Faculty of Biology, Warsaw University intramural grant, BW 501/86-100047. We are grateful to Dr Tomasz Krupnik for the English correction of the manuscript.

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Correspondence to Romanowska Elżbieta.

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Wioleta, W., Anna, D., Ilona, B. et al. Lead induced changes in phosphorylation of PSII proteins in low light grown pea plants. Biometals 28, 151–162 (2015). https://doi.org/10.1007/s10534-014-9811-y

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  • DOI: https://doi.org/10.1007/s10534-014-9811-y

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