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Light-harvesting complex II protein CP29 binds to photosystem I of Chlamydomonas reinhardtii under State 2 conditions
Wolfson Laboratories, Division of Molecular Biosciences, Imperial College London, UK .
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Cellbiologi. Linköpings universitet, Hälsouniversitetet.
Wolfson Laboratories, Division of Molecular Biosciences, Imperial College London, UK .
Wolfson Laboratories, Division of Molecular Biosciences, Imperial College London, UK .
Visa övriga samt affilieringar
2005 (Engelska)Ingår i: The FEBS journal, ISSN 1742-464X, Vol. 272, nr 18, s. 4797-4806Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The State 1 to State 2 transition in the photosynthetic membranes of plants and green algae involves the functional coupling of phosphorylated light-harvesting complexes of photosystem II (LHCII) to photosystem I (PSI). We present evidence suggesting that in Chlamydomonas reinhardtii this coupling may be aided by a hyper-phosphorylated form of the LHCII-like CP29 protein (Lhcbm4). MS analysis of CP29 showed that Thr6, Thr16 and Thr32, and Ser102 are phosphorylated in State 2, whereas in State 1-exposed cells only phosphorylation of Thr6 and Thr32 could be detected. The LHCI–PSI supercomplex isolated from the alga in State 2 was found to contain strongly associated CP29 in phosphorylated form. Electron microscopy suggests that the binding site for this highly phosphorylated CP29 is close to the PsaH protein. It is therefore postulated that redox-dependent multiple phosphorylation of CP29 in green algae is an integral part of the State transition process in which the structural changes of CP29, induced by reversible phosphorylation, determine the affinity of LHCII for either of the two photosystems.

Ort, förlag, år, upplaga, sidor
2005. Vol. 272, nr 18, s. 4797-4806
Nyckelord [en]
Chlamydomonas, CP29, photosynthesis, protein phosphorylation, State transitions
Nationell ämneskategori
Medicin och hälsovetenskap
Identifikatorer
URN: urn:nbn:se:liu:diva-12929DOI: 10.1111/j.1742-4658.2005.04894.xOAI: oai:DiVA.org:liu-12929DiVA, id: diva2:17415
Tillgänglig från: 2008-02-06 Skapad: 2008-02-06
Ingår i avhandling
1. Functional proteomics of protein phosphorylation in algal photosynthetic membranes
Öppna denna publikation i ny flik eller fönster >>Functional proteomics of protein phosphorylation in algal photosynthetic membranes
2008 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

Plants, green algae and cyanobacteria perform photosynthetic conversion of sunlight into chemical energy in the permanently changing natural environment. For successful survival and growth photosynthetic organisms have developed complex sensing and signaling acclimation mechanisms. The environmentally dependent protein phosphorylation in photosynthetic membranes is implied in the adaptive responses; however, the molecular mechanisms of this regulation are still largely unknown. We used a mass spectrometry-based approach to achieve a comprehensive mapping of the in vivo protein phosphorylation sites within photosynthetic membranes from the green alga Chlamydomonas reinhardtii subjected to distinct environmental conditions known to affect the photosynthetic machinery.

The state transitions process regulating the energy distribution between two photosystems, involves the temporal functional coupling of phosphorylated light-harvesting complexes II (LHCII) to photosystem I (PSI). During state transitions several of the thylakoid proteins undergo redox-controlled phosphorylation-dephosphorylation cycles. This work provided evidences suggesting that redox-dependent phosphorylation-induced structural changes of the minor LHCII antenna protein CP29 determine the affinity of LHCII for either of the two photosystems. In state 1 the doubly phosphorylated CP29 acts as a linker between the photosystem II (PSII) core and the trimeric LHCII whereas in state 2 this quadruply phosphorylated CP29 would migrate to PSI on the PsaH side and provide the docking of LHCII trimers to the PSI complex. Moreover, this study revealed that exposure of Chlamydomonas cells to high light stress caused hyperphosphorylation of CP29 at seven distinct residues and suggested that high light-induced hyperphosphorylation of CP29 may uncouple this protein together with LHCII from both photosystems to minimize the damaging effects of excess light.

Reversible phosphorylation of the PSII reaction center proteins was shown to be essential for the maintenance of active PSII under high light stress. Particularly dephosphorylation of the light-damaged D1 protein, a central functional subunit of the PSII reaction center, is required for its degradation and replacement. We found in the alga the reversible D1 protein phosphorylation, which until our work, has been considered as plant-specific.

We also discovered specific induction of thylakoid protein phosphorylation during adaptation of alga to limiting environmental CO2. One of the phosphorylated proteins has five phosphorylation sites at both serine and treonine residues. The discovered specific low-CO2- and redox-dependent protein phosphorylation may be an early adaptive and signalling response of the green alga to limitation in inorganic carbon.

This work provides the first comprehensive insight into the network of environmentally regulated protein phosphorylation in algal photosynthetic membranes.

Ort, förlag, år, upplaga, sidor
Linköping University Electronic Press, 2008. s. 40
Serie
Linköping University Medical Dissertations, ISSN 0345-0082 ; 1038
Nyckelord
Protein phosphorylation, mass spectrometry, photosynthesis, proteomics
Nationell ämneskategori
Biokemi och molekylärbiologi
Identifikatorer
urn:nbn:se:liu:diva-10708 (URN)978-91-85523-02-3 (ISBN)
Disputation
2008-02-29, Linden, ingång 65, Hälsouniversitetet, Linköping, 13:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2008-02-06 Skapad: 2008-02-06 Senast uppdaterad: 2015-11-19

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Turkina, Maria VVener, Alexander V

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