Phosphorylation of Photosystem II Proteins

Rintamäki, Eevi; Aro, Eva‐Mari

doi:10.1007/0-306-48148-0_23

Cited by 12 publications

(19 citation statements)

References 171 publications

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“…Most thylakoid phosphoproteins are singly phosphorylated, and only the 9-kDa PsbH gene product has two phosphorylation sites (12,43). The previously characterized thylakoid phosphoproteins constitute the major photosynthetic protein complexes (12,13,(20)(21)(22), and the phosphorylation sites in analogous proteins from different plants are rather conserved (19). Comparison of the protein sequences deduced from ESTs of 20 different plants with spinach TSP9 does not show a high conservation for the phosphorylated threonine residues.…”

Section: Discussionmentioning

confidence: 96%

“…The possible absence of TSP9 in algae could give this phosphoprotein a unique place in the protein phosphorylation network of oxygenic photosynthetic organisms. Phosphorylation of PSII proteins is absent in cyanobacteria but occurs in plants and green algae (19). TSP9 could represent a distinction between the regulatory phosphorylation in algae and plants.…”

Section: Discussionmentioning

confidence: 99%

“…The reversible phosphorylation of LHCII polypeptides helps balance the distribution of absorbed light energy between the two photosystems (1,(15)(16)(17). Phosphorylation of the core subunits of PSII controls their maintenance and turnover, with dephosphorylation of the D1 and D2 proteins being a signal for their proteolytic degradation (18,19). Two other subunits of PSII, the chlorophyll a-binding protein CP43 and the 9-kDa PsbH gene product, are also phosphorylated in thylakoid membranes (20, 21).…”

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confidence: 99%

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A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes

Carlberg

Hansson

Kieselbach

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of Arabidopsis and rice as well as in ESTs from 20 different plant species, but not from any other organisms. The protein can be released from the membrane with high salt and is also partially released in response to light-induced phosphorylation of thylakoids, in contrast to all other known thylakoid phosphoproteins, which are integral to the membrane. On the basis of its properties, this plant-specific protein is named thylakoid soluble phosphoprotein of 9 kDa (TSP9). Mass spectrometric analyses revealed the existence of non-, mono-, di-, and triphosphorylated forms of TSP9 and phosphorylation of three distinct threonine residues in the central part of the protein. The phosphorylation and release of TSP9 from the photosynthetic membrane on illumination favor participation of this basic protein in cell signaling and regulation of plant gene expression in response to changing light conditions. P rotein phosphorylation plays a major regulatory role in all cellular functions, from gene expression to signaling and metabolic control. A unique light-and redox-controlled protein phosphorylation system has evolved in plant thylakoid membranes for regulation of the photosynthetic process (1, 2). Intrinsic protein kinases in chloroplast thylakoid membranes (3-5) are activated by light or reducing conditions and controlled by the reduction of plastoquinone and its binding to the reduced cytochrome bf complex (6, 7). Additional modulation of protein phosphorylation in thylakoid membranes involves the thiol redox state (8, 9) as well as light-modulated conformational changes of substrate proteins (10). Activated thylakoid kinases phosphorylate the membrane proteins of photosystem II (PSII) and its light-harvesting antenna (LHCII) as well as a number of still unidentified protein substrates (2, 11-13). The protein dephosphorylation reactions are catalyzed by both integral thylakoid membrane and soluble chloroplast phosphatases (2, 14). The reversible phosphorylation of LHCII polypeptides helps balance the distribution of absorbed light energy between the two photosystems (1,(15)(16)(17). Phosphorylation of the core subunits of PSII controls their maintenance and turnover, with dephosphorylation of the D1 and D2 proteins being a signal for their proteolytic degradation (18,19). Two other subunits of PSII, the chlorophyll a-binding ...

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes

Carlberg

Hansson

Kieselbach

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…Particularly dephosphorylation of the light-damaged D1 protein, a central functional subunit of the PSII reaction center, is required for its degradation and replacement (13)(14)(15). It is worth noting that until our present work, reversible phosphorylation of the D1 protein has been considered as plant-specific (13,15,16).…”

mentioning

confidence: 87%

“…Reversible phosphorylation of the PSII reaction center proteins has been found essential for the maintenance of active PSII under high light stress (11)(12)(13). Particularly dephosphorylation of the light-damaged D1 protein, a central functional subunit of the PSII reaction center, is required for its degradation and replacement (13)(14)(15).…”

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confidence: 99%

Environmentally Modulated Phosphoproteome of Photosynthetic Membranes in the Green Alga Chlamydomonas reinhardtii

Turkina

Kargul

Blanco-Rivero

et al. 2006

Molecular & Cellular Proteomics

108

119

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Mapping of in vivoThe thylakoid membranes in chloroplasts of plants and green algae carry out oxygenic photosynthesis. Two multisubunit pigment-containing protein complexes, photosystem II (PSII) 1 and photosystem I (PSI), located in this membrane system work in series to generate an electrochemical potential gradient of protons across the membrane following vectorial electron flow from PSII to PSI via the cytochrome b 6 f complex. PSII uses light to oxidize water, whereas PSI, via a second photoact, uses reducing equivalents derived from PSII to reduce NADP ϩ to NADPH. The electrochemical potential gradient of protons is used to power conversion of ADP to ATP (1). Several thylakoid membrane proteins that make up the PSII complex and its LHCII (light-harvesting chlorophyll a/b-binding proteins of PSII) antennae undergo light-and redox-dependent phosphorylation (2, 3) as discovered more than 2 decades ago (4 -6). Phosphorylation of LHCII in plants and algae controls photosynthetic state transitions, which optimize efficient use of the absorbed light energy by both photosystems. Thus, in State 1 more energy is transferred to PSII, whereas in State 2 a proportion of the excitation energy is redistributed to PSI (7-9). The essential role of protein phosphorylation in state transitions has recently been proven in the studies using mutants of Arabidopsis thaliana plants and the green alga Chlamydomonas reinhardtii deficient in protein kinases STN7 (9) and Stt7 (8), respectively. However, despite the generally assumed similarity in thylakoid protein phosphorylation between plants and algae and a high homology between the plant STN7 and the algal Stt7 protein kinases (8), the extent of photosynthetic state transitions differs between these species. In plant thylakoids, only 15-20% of LHCII participates in the lateral migration between the photosystems, whereas up to 80% of the excitation energy absorbed by the LHCII antenna can be redistributed from PSII to PSI in green alga (8 -10).

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Change of proton motive force across thylakoid membrane in soybean leaf during state transitions

2003

Sci. Bull.

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Phosphorylation of Photosystem II Proteins

Cited by 12 publications

References 171 publications

A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes

A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes

Environmentally Modulated Phosphoproteome of Photosynthetic Membranes in the Green Alga Chlamydomonas reinhardtii

Change of proton motive force across thylakoid membrane in soybean leaf during state transitions

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