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- Damkjaer, Jakob, 1976-
(author)
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Phosphorylation in State Transition : Less cause more effect
- 2011
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Doctoral thesis (other academic/artistic)abstract
- Study of the Arabidopsis thaliana knockout mutant lacking Lhcb3 (koLhcb3) have revealed a close similarity to the wild type plants. Growth rate, NPQ, qP, Φ(PSII), circular dichroism spectra, pigment composition and content of LCHII trimers have been found to be unaffected by this mutation. The proteomic analysis shows only some minor increases in the amount of Lhcb1 and Lhcb2. PAM fluorometry revealed a significant increase in the rate of the state 1 to state 2 state transition in the koLhcb3. None the less, the extent of state transition is identical to wild type. Alterations in the PSII-LHCII supercomplex structure have been demonstrated as well. The M-trimer was found to be rotated ~21° CCW. This altered binding of the LHCII M-trimer is likely the cause of the altered affinity resulting in the increased rate of state transition. Proteomic analysis of the phosphorylation of LHCII revealed a significant increase in state 1 and 2 LHCII phosphorylation relative to wild type. Investigation whether phosphorylation or the altered LHCII binding is the cause of the accelerated rate of state transition have not been conclusive so far. A Lhcb6 depleted mutant (koLhcb6) showed a significant alteration of the PSII-LHCII supercomplex structure and photosynthetic acclimation processes. The LHCII M-trimer is depleted in the PSII-LHCII supercomplexes causing the state transition process to be “stuck” in state 2 and the mutants ability to preform NPQ is inhibited as well. The Lhcb6 protein was concluded to be essential for the binding of the LHCII M-trimer to the PSII core as well as energy transfer. The depletion of LHCII M-trimer was linked to the reduced ability to photoacclimate using NPQ as well.
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| 2. |
- Garcia Cerdan, Jose Gines, 1977-
(author)
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Functions of REP27 and the low molecular weight proteins PsbX and PsbW in repair and assembly of photosystem II
- 2009
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Doctoral thesis (other academic/artistic)abstract
- Oxygenic photosynthesis is the major producer of both oxygen and organic compounds on earth and takes place in plants, green algae and cyanobacteria. The thylakoid membranes are the site of the photosynthetic light reactions that involve the concerted action of four major protein complexes known as photosystem II (PSII), cytochrome b6f complex, ATP synthase and photosystem I (PSI). The function of PSII is of particular interest as it performs the light–driven water splitting reaction driving the photosynthetic electron transport. My thesis addressed different aspects of PSII assembly and the functions of its low molecular weight PSII subunits PsbX and PsbW. Photosynthesis in green algae and higher plants is controlled by the nucleus. Many proteins of nuclear origin participate in the regulation of the efficient assembly of the photosynthetic protein complexes. In this investigation we have identified one of these nuclear encoded auxiliary proteins of photosystem II, REP27, which participates in the assembly of the D1 reaction center protein and repair of photodamaged PSII in the green algae Chlamydomonas reinhardtii. Interestingly, PSII is specially enriched in Low Molecular Weight (LMW) subunits that have masses less than 10kDa. These proteins account for more than the half of the PSII subunits. Several questions remains poorly understood regarding the LMW: Which is their evolutionary origin? What function do they perform in the protein complex? Where are they located in the protein structure? In this investigation the functions of two of these LMW subunits (PsbX and PsbW) have been studied using antisense inhibition and T-DNA knockout mutant plants in Arabidopsis thaliana. Deficiency of the PsbX protein leads to impaired accumulation and functionality of PSII. Characterization of PsbW knock-out plants show that PsbW participates in stabilization of the macro-organization of PSII and the peripheral antenna (Light Harvesting Complex, LHCII) in the grana stacks of the chloroplast, also known as PSII-LHCII supercomplexes.
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