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Lack of the light-harvesting complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts.
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
Department of Biophysical Chemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands.
Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom.
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2006 (English)In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 18, no 11, 3106-20 p.Article in journal (Refereed) Published
Abstract [en]

The photosystem II (PSII) light-harvesting antenna in higher plants contains a number of highly conserved gene products whose function is unknown. Arabidopsis thaliana plants depleted of one of these, the CP24 light-harvesting complex, have been analyzed. CP24-deficient plants showed a decrease in light-limited photosynthetic rate and growth, but the pigment and protein content of the thylakoid membranes were otherwise almost unchanged. However, there was a major change in the macroorganization of PSII within these membranes; electron microscopy and image analysis revealed the complete absence of the C2S2M2 light-harvesting complex II (LHCII)/PSII supercomplex predominant in wild-type plants. Instead, only C2S2 supercomplexes, which are deficient in the LHCIIb M-trimers, were found. Spectroscopic analysis confirmed the disruption of the wild-type macroorganization of PSII. It was found that the functions of the PSII antenna were disturbed: connectivity between PSII centers was reduced, and maximum photochemical yield was lowered; rapidly reversible nonphotochemical quenching was inhibited; and the state transitions were altered kinetically. CP24 is therefore an important factor in determining the structure and function of the PSII light-harvesting antenna, providing the linker for association of the M-trimer into the PSII complex, allowing a specific macroorganization that is necessary both for maximum quantum efficiency and for photoprotective dissipation of excess excitation energy.

Place, publisher, year, edition, pages
2006. Vol. 18, no 11, 3106-20 p.
Keyword [en]
Arabidopsis/*metabolism/radiation effects/ultrastructure, Arabidopsis Proteins/analysis/isolation & purification/*metabolism, Chloroplasts/*ultrastructure, Chromatography; Gel, Circular Dichroism, DNA; Bacterial/metabolism, Fluorescence, Light, Light-Harvesting Protein Complexes/analysis/*deficiency/isolation & purification, Models; Biological, Mutagenesis; Insertional, Photosynthesis/radiation effects, Photosynthetic Reaction Center Complex Proteins/metabolism, Photosystem II Protein Complex/metabolism, Pigments; Biological/metabolism, Plant Leaves/radiation effects, RNA; Antisense/metabolism, Structure-Activity Relationship, Temperature, Thylakoids/*ultrastructure
URN: urn:nbn:se:umu:diva-14197DOI: 10.1105/tpc.106.045641PubMedID: 17114352OAI: diva2:153868
Available from: 2007-05-24 Created: 2007-05-24 Last updated: 2015-04-29Bibliographically approved
In thesis
1. Phosphorylation in State Transition: Less cause more effect
Open this publication in new window or tab >>Phosphorylation in State Transition: Less cause more effect
2011 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Fosforylering och "state transitions" : mindre orsak, mer verkan
Abstract [en]

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.

Place, publisher, year, edition, pages
University of Umeå: Department of Plant Physiology, 2011. 56 p.
Photosynthesis, Photoacclimation, State Transtion, LHCII Phosphorylation, Lhcb3, Lhcb6
National Category
Research subject
Molecular Biology
urn:nbn:se:umu:diva-38870 (URN)978-91-7459-131-6 (ISBN)
Public defence
2011-01-28, Naturvetarhuset, N450, Umeå Universitet, Umeå, 10:00 (English)
Available from: 2011-01-05 Created: 2011-01-05 Last updated: 2015-04-29Bibliographically approved

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Damkjaer, JakobJansson, Stefan
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