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Phosphorylation of Photosystem II Controls Functional Macroscopic Folding of Photosynthetic Membranes in Arabidopsis
Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
Departments of Molecular Biology and Plant Biology, University of Geneva, CH-1211 Geneva 4, Switzerland.
Linköping University, Department of Clinical and Experimental Medicine. Linköping University, Faculty of Health Sciences.
Departments of Molecular Biology and Plant Biology, University of Geneva, CH-1211 Geneva 4, Switzerland.
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2009 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 21, no 12, 3950-3964 p.Article in journal (Refereed) Published
Abstract [en]

Photosynthetic thylakoid membranes in plants contain highly folded membrane layers enriched in photosystem II, which uses light energy to oxidize water and produce oxygen. The sunlight also causes quantitative phosphorylation of major photosystem II proteins. Analysis of the Arabidopsis thaliana stn7xstn8 double mutant deficient in thylakoid protein kinases STN7 and STN8 revealed light-independent phosphorylation of PsbH protein and greatly reduced N-terminal phosphorylation of D2 protein. The stn7xstn8 and stn8 mutants deficient in light-induced phosphorylation of photosystem II had increased thylakoid membrane folding compared with wild-type and stn7 plants. Significant enhancement in the size of stacked thylakoid membranes in stn7xstn8 and stn8 accelerated gravity-driven sedimentation of isolated thylakoids and was observed directly in plant leaves by transmission electron microscopy. Increased membrane folding, caused by the loss of light-induced protein phosphorylation, obstructed lateral migration of the photosystem II reaction center protein D1 and of processing protease FtsH between the stacked and unstacked membrane domains, suppressing turnover of damaged D1 in the leaves exposed to highlight. These findings show that the high level of photosystem II phosphorylation in plants is required for adjustment of macroscopic folding of large photosynthetic membranes modulating lateral mobility of membrane proteins and sustained photosynthetic activity.

Place, publisher, year, edition, pages
2009. Vol. 21, no 12, 3950-3964 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-54057DOI: 10.1105/tpc.109.069435ISI: 000274196000019OAI: oai:DiVA.org:liu-54057DiVA: diva2:298321
Available from: 2010-02-22 Created: 2010-02-22 Last updated: 2017-12-12
In thesis
1. Regulatory Functions of Protein Phosphorylation in Plant Photosynthetic Membranes
Open this publication in new window or tab >>Regulatory Functions of Protein Phosphorylation in Plant Photosynthetic Membranes
2010 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Oxygenic photosynthesis is the process in plants, algae and cyanobacteria which converts light energy from the sun into carbohydrates and at the same time produces oxygen from water. Both carbohydrates and oxygen are essential to sustain life on earth. Sunlight is thus a necessity for life, but it can also cause severe problems for photosynthetic organisms, which have evolved several remarkable acclimation systems to cope with light fluctuations in the environment. In higher plants the light driven reactions of photosynthesis proceed in the chloroplast thylakoid membranes highly organized into stacked regions of grana and interconnecting stroma  lamellae. The grana structure is thought to provide functional benefits in the processes of acclimation of the photosynthetic apparatus, particularly in the quality control of photosystem II (PSII) were photodamaged PSII is repaired in a stepwise manner. These processes in the thylakoid membranes were suggested to be regulated by reversible phosphorylation of several proteins in PSII and in its light harvesting antennae complexes (LHCII). Two thylakoid protein kinases, called STN8 and STN7, have been previously identified as responsible for the phosphorylation of PSII and LHCII, respectively. However, molecular mechanisms and the exact functions of these protein phosphorylation events remained largely unknown.

In this thesis research I have demonstrated that the PSII protein phosphorylation is needed for the maintenance of the thylakoid structure in Arabidopsis thaliana chloroplasts. A big part of the work on characterization of proteins and their phosphorylation has been done using novel mass spectrometry techniques, and we further developed a label-free method for quantitative studies of protein phosphorylation. The phosphorylation of PSII proteins was found to be diurnal regulated and required for maintenance of the cation-dependent functional stacking of the thylakoid membranes. This phosphorylation was further shown to be important for the regulated turnover of the D1 protein of PSII.

Phosphorylation of the plant specific TSP9 protein was found to be dependent on STN7 kinase, and plants deficient in TSP9 showed reduced ability to perform the photosynthetic state transitions and to execute thermal dissipation of excess light energy under high light conditions. I also accomplished characterization of the protein phosphorylation in thylakoids from Arabidopsis plants subjected to high light treatment and discovered STN7-dependent phosphorylation of the antenna protein CP29 required for the adaptive disassembly of PSII supercomplexes in conditions of high light stress.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2010. 42 p.
Series
Linköping University Medical Dissertations, ISSN 0345-0082 ; 1212
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-62303 (URN)978-91-7393-301-8 (ISBN)
Public defence
2010-12-17, Linden, Hälsouniversitetet, Campus US, Linköpings universitet, Linköping, 13:00 (English)
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Available from: 2010-11-26 Created: 2010-11-26 Last updated: 2010-11-26Bibliographically approved

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Fristedt, RikardVener, Alexander

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