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Environmentally modulated phosphoproteome of photosynthetic membranes in the green alga Chlamydomonas reinhardtii
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Umeå University, Faculty of Science and Technology, Department of Plant Physiology.
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2006 (English)In: Molecular & Cellular Proteomics, ISSN 1535-9476, E-ISSN 1535-9484, Vol. 5, no 8, 1412-1425 p.Article in journal (Refereed) Published
Abstract [en]

Mapping of in vivo protein phosphorylation sites in photosynthetic membranes of the green alga Chlamydomonas reinhardtii revealed that the major environmentally dependent changes in phosphorylation are clustered at the interface between the photosystem II (PSII) core and its light-harvesting antennae (LHCII). The photosynthetic membranes that were isolated form the algal cells exposed to four distinct environmental conditions affecting photosynthesis: (i) dark aerobic, corresponding to photosynthetic State 1; (ii) dark under nitrogen atmosphere, corresponding to photosynthetic State 2; (iii) moderate light; and (iv) high light. The surface-exposed phosphorylated peptides were cleaved from the membrane by trypsin, methyl-esterified, enriched by immobilized metal affinity chromatography, and sequenced by nanospray-quadrupole time-of-flight mass spectrometry. A total of 19 in vivo phosphorylation sites were mapped in the proteins corresponding to 15 genes in C. reinhardtii. Amino-terminal acetylation of seven proteins was concomitantly determined. Sequenced amino termini of six mature LHCII proteins differed from the predicted ones. The State 1-to-State 2 transition induced phosphorylation of the PSII core components D2 and PsbR and quadruple phosphorylation of a minor LHCII antennae subunit, CP29, as well as phosphorylation of constituents of a major LHCII complex, Lhcbm1 and Lhcbm10. Exposure of the algal cells to either moderate or high light caused additional phosphorylation of the D1 and CP43 proteins of the PSII core. The high light treatment led to specific hyperphosphorylation of CP29 at seven distinct residues, phosphorylation of another minor LHCII constituent, CP26, at a single threonine, and double phosphorylation of additional subunits of a major LHCII complex including Lhcbm4, Lhcbm6, Lhcbm9, and Lhcbm11. Environmentally induced protein phosphorylation at the interface of PSII core and the associated antenna proteins, particularly multiple differential phosphorylations of CP29 linker protein, suggests the mechanisms for control of photosynthetic state transitions and for LHCII uncoupling from PSII under high light stress to allow thermal energy dissipation.

Place, publisher, year, edition, pages
Bethesda: American society of biochemistry and molecular biology , 2006. Vol. 5, no 8, 1412-1425 p.
Keyword [en]
light-harvesting complex, thylakoid protein-phosphorylation, oxygen-evolving complex, plant photosystem-II, state transitions, mass-spectrometry, in vivo, arabidopsis thaliana, reversible phosphorylation, 3-dimensional structure
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:umu:diva-18887DOI: 10.1074/mcp.M600066-MCP200ISI: 000239627800005PubMedID: 16670252OAI: diva2:175029
Available from: 2009-02-26 Created: 2009-02-26 Last updated: 2016-08-11Bibliographically approved

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Blanco-Rivero, AmayaVillarejo, Arsenio
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Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)
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