Functional analysis of LHCSR1, a protein catalyzing NPQ in mosses, by heterologous expression in Arabidopsis thaliana View Full Text


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Article Info

DATE

2019-07-03

AUTHORS

Ioannis Dikaios, Christo Schiphorst, Luca Dall’Osto, Alessandro Alboresi, Roberto Bassi, Alberta Pinnola

ABSTRACT

Non-photochemical quenching, NPQ, of chlorophyll fluorescence regulates the heat dissipation of chlorophyll excited states and determines the efficiency of the oxygenic photosynthetic systems. NPQ is regulated by a pH-sensing protein, responding to the chloroplast lumen acidification induced by excess light, coupled to an actuator, a chlorophyll/xanthophyll subunit where quenching reactions are catalyzed. In plants, the sensor is PSBS, while the two pigment-binding proteins Lhcb4 (also known as CP29) and LHCII are the actuators. In algae and mosses, stress-related light-harvesting proteins (LHCSR) comprise both functions of sensor and actuator within a single subunit. Here, we report on expressing the lhcsr1 gene from the moss Physcomitrella patens into several Arabidopsis thaliana npq4 mutants lacking the pH sensing PSBS protein essential for NPQ activity. The heterologous protein LHCSR1 accumulates in thylakoids of A. thaliana and NPQ activity can be partially restored. Complementation of double mutants lacking, besides PSBS, specific xanthophylls, allowed analyzing chromophore requirement for LHCSR-dependent quenching activity. We show that the partial recovery of NPQ is mostly due to the lower levels of Zeaxanthin in A. thaliana in comparison to P. patens. Complemented npq2npq4 mutants, lacking besides PSBS, Zeaxanthin Epoxidase, showed an NPQ recovery of up to 70% in comparison to A. thaliana wild type. Furthermore, we show that Lutein is not essential for the folding nor for the quenching activity of LHCSR1. In short, we have developed a system to study the function of LHCSR proteins using heterologous expression in a variety of A. thaliana mutants. More... »

PAGES

249-264

References to SciGraph publications

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  • 2006-12-27. Lutein is needed for efficient chlorophyll triplet quenching in the major LHCII antenna complex of higher plants and effective photoprotection in vivounder strong light in BMC PLANT BIOLOGY
  • 2017-07-17. Single-molecule spectroscopy of LHCSR1 protein dynamics identifies two distinct states responsible for multi-timescale photosynthetic photoprotection in NATURE CHEMISTRY
  • 2000-01. A pigment-binding protein essential for regulation of photosynthetic light harvesting in NATURE
  • 2017-09-11. Functional modulation of LHCSR1 protein from Physcomitrella patens by zeaxanthin binding and low pH in SCIENTIFIC REPORTS
  • 2009-11. An ancient light-harvesting protein is critical for the regulation of algal photosynthesis in NATURE
  • 1990-09. The relationship between non-photochemical quenching of chlorophyll fluorescence and the rate of photosystem 2 photochemistry in leaves in PHOTOSYNTHESIS RESEARCH
  • 2007-11. Identification of a mechanism of photoprotective energy dissipation in higher plants in NATURE
  • 2006-06-29. Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method in NATURE PROTOCOLS
  • 1999-05. How acidic is the lumen? in PHOTOSYNTHESIS RESEARCH
  • 1979-01. Analysis of gametophytic development in the moss, Physcomitrella patens, using auxin and cytokinin resistant mutants in PLANTA
  • 2017-04-10. Two mechanisms for dissipation of excess light in monomeric and trimeric light-harvesting complexes in NATURE PLANTS
  • 2004-06. Cyclic electron flow around photosystem I is essential for photosynthesis in NATURE
  • 2010-01-12. Purification of structurally intact grana from plants thylakoids membranes in JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s11120-019-00656-3

    DOI

    http://dx.doi.org/10.1007/s11120-019-00656-3

    DIMENSIONS

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    PUBMED

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    36 schema:description Non-photochemical quenching, NPQ, of chlorophyll fluorescence regulates the heat dissipation of chlorophyll excited states and determines the efficiency of the oxygenic photosynthetic systems. NPQ is regulated by a pH-sensing protein, responding to the chloroplast lumen acidification induced by excess light, coupled to an actuator, a chlorophyll/xanthophyll subunit where quenching reactions are catalyzed. In plants, the sensor is PSBS, while the two pigment-binding proteins Lhcb4 (also known as CP29) and LHCII are the actuators. In algae and mosses, stress-related light-harvesting proteins (LHCSR) comprise both functions of sensor and actuator within a single subunit. Here, we report on expressing the lhcsr1 gene from the moss Physcomitrella patens into several Arabidopsis thaliana npq4 mutants lacking the pH sensing PSBS protein essential for NPQ activity. The heterologous protein LHCSR1 accumulates in thylakoids of A. thaliana and NPQ activity can be partially restored. Complementation of double mutants lacking, besides PSBS, specific xanthophylls, allowed analyzing chromophore requirement for LHCSR-dependent quenching activity. We show that the partial recovery of NPQ is mostly due to the lower levels of Zeaxanthin in A. thaliana in comparison to P. patens. Complemented npq2npq4 mutants, lacking besides PSBS, Zeaxanthin Epoxidase, showed an NPQ recovery of up to 70% in comparison to A. thaliana wild type. Furthermore, we show that Lutein is not essential for the folding nor for the quenching activity of LHCSR1. In short, we have developed a system to study the function of LHCSR proteins using heterologous expression in a variety of A. thaliana mutants.
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