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Structure and function of the lightharvesting complex of higher plant photosystem I
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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(English)Manuscript (preprint) (Other academic)
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URN: urn:nbn:se:umu:diva-3782OAI: diva2:142651
Available from: 2004-03-12 Created: 2004-03-12 Last updated: 2015-04-29Bibliographically approved
In thesis
1. The light-harvesting antenna of higher plant photosystem I
Open this publication in new window or tab >>The light-harvesting antenna of higher plant photosystem I
2004 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

During photosynthesis, two multi-protein complexes, photosystems (PS) I and II work in tandem to convert the light-energy absorbed by the light-harvesting antennae into chemical energy, which is subsequently used to assimilate atmospheric carbon dioxide into organic carbon compounds. This is the main nutritional basis for life on Earth.

The photosynthetic antenna of higher plants comprises at least ten different pigment-binding proteins (LHC), which play important roles in photosynthesis. Chlorophyll and carotenoid molecules associated with the LHC proteins are organised into an array, which can be modulated, thereby optimising light-harvesting processes and protection against oxidative damage under conditions of excessive light absorption. All ten LHC proteins have been conserved through eons of evolution, suggesting that there are strong evolutionary pressures to retain all ten proteins, and hence that each protein has a unique function.

The light-harvesting antenna of higher plant PSI consists of at least four proteins, Lhca1-4, collectively called LHCI. By constructing transgenic Arabidopsis thaliana plants in which each Lhca gene has been individually repressed or knocked-out, a collection of plants with different Lhca protein contents was obtained. The objective was to use these plants to study the structure, function and regulation of the Lhca proteins in vivo. The major findings of this work are as follows.

Removing single Lhca proteins influenced the stability of the other Lhca proteins, showing that there is a high degree of inter-dependency between the polypeptides in LHCI, and hence that a full set of Lhca proteins is important for maintaining the structural integrity of LHCI. This has provided insight into the organisation of LHCI by revealing clues about the relative positions of each Lhca protein in the antenna complex. The physiological consequences of removing individual Lhca proteins were dependent on the degree of antenna depletion. Plants with relatively small antenna changes could compensate, to some extent, for the loss of LHCI, while larger depletions had profound effects on whole plant resulting in growth reductions.

The fitness of each Lhca plant was assessed by measuring their seed production in the harsh conditions in the field. We found that all Lhca-deficient plants produced fewer seeds under some conditions, with seed-production compared to wild type varying between 10-80% depending on the extent of LHCI reduction. Therefore, we conclude that each Lhca protein is important for plant fitness, and hence for the survival of the species.

PSI is characterised by a pool of pigments absorbing light in the red end of the solar visible spectrum, thought to be especially important for plants in dense vegetation systems where the incident light is enriched in wavelengths higher than 690 nm. A majority of these pigments are situated on LHCI and, based on in-vitro studies, were thought to be mainly associated with Lhca4. Using our plants, we have established that red pigments are indeed present on all Lhca proteins and that these pigments become even more red upon association with PSI.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2004. 67 p.
Plant physiology, antisense, Arabidopsis thaliana, chlorophyll, fitness, LHC, photosynthesis, Växtfysiologi
National Category
urn:nbn:se:umu:diva-209 (URN)91-7305-625-1 (ISBN)
Public defence
2004-04-02, Umeå, 10:00
Available from: 2004-03-12 Created: 2004-03-12 Last updated: 2011-03-10Bibliographically approved

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Klimmek, FrankJansson, Stefan
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Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)

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