title: The effect of zeaxanthin as the only xanthophyll on the structure and function of the photosynthetic apparatus in Arabidopsis thaliana.
abstract: In green plants, the xanthophyll carotenoid zeaxanthin is synthesized transiently under conditions of excess light energy and participates in photoprotection. In the Arabidopsis lut2 npq2 double mutant, all xanthophylls were replaced constitutively by zeaxanthin, the only xanthophyll whose synthesis was not impaired. The relative proportions of the different chlorophyll antenna proteins were strongly affected with respect to the wild-type strain. The major antenna, LHCII, did not form trimers, and its abundance was strongly reduced as was CP26, albeit to a lesser extent. In contrast, CP29, CP24, LHCI proteins, and the PSI and PSII core complexes did not undergo major changes. PSII-LHCII supercomplexes were not detectable while the PSI-LHCI supercomplex remained unaffected. The effect of zeaxanthin accumulation on the stability of the different Lhc proteins was uneven: the LHCII proteins from lut2 npq2 had a lower melting temperature as compared with the wild-type complex while LHCI showed increased resistance to heat denaturation. Consistent with the loss of LHCII, light-state 1 to state 2 transitions were suppressed, the photochemical efficiency in limiting light was reduced and photosynthesis was saturated at higher light intensities in lut2 npq2 leaves, resulting in a photosynthetic phenotype resembling that of high light-acclimated leaves. Zeaxanthin functioned in vivo as a light-harvesting accessory pigment in lut2 npq2 chlorophyll antennae. As a whole, the in vivo data are consistent with the results obtained by using recombinant Lhc proteins reconstituted in vitro with purified zeaxanthin. While PSII photoinhibition was similar in wild type and lut2 npq2 exposed to high light at low temperature, the double mutant was much more resistant to photooxidative stress and lipid peroxidation than the wild type. The latter observation is consistent with an antioxidant and lipid protective role of zeaxanthin in vivo.
authors.affiliation: CEA/Cadarache, DSV, DEVM, Laboratoire d'Ecophysiologie de la Photosynthèse, UMR 163 CEA-CNRS, Université Méditérranée-CEA 1000, F-13108 Saint-Paul-lez-Durance, France. michel.havaux@cea.fr
authors.forename: Michel
authors.initials: M
authors.lastname: Havaux
authors.forename: Luca
authors.initials: L
authors.lastname: Dall'Osto
authors.forename: Stephan
authors.initials: S
authors.lastname: Cuiné
authors.forename: Giovanni
authors.initials: G
authors.lastname: Giuliano
authors.forename: Roberto
authors.initials: R
authors.lastname: Bassi
mesh_terms: D000064:Acclimatization / Q000502:physiology; D001059:Apoproteins / Q000378:metabolism; D017360:Arabidopsis / Q000502:physiology*; D004579:Electron Transport; D009154:Mutation; D018384:Oxidative Stress / Q000502:physiology; D010641:Phenotype; D010788:Photosynthesis / Q000502:physiology*; D045332:Photosystem II Protein Complex / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018515:Plant Leaves / Q000502:physiology; D010940:Plant Proteins; D017434:Protein Structure, Tertiary; D024341:Xanthophylls; D065146:Zeaxanthins; D019207:beta Carotene / Q000031:analogs & derivatives / Q000235:genetics* / Q000378:metabolism*
chemical_list: D001059:Apoproteins; D045332:Photosystem II Protein Complex; D010940:Plant Proteins; D024341:Xanthophylls; D065146:Zeaxanthins; D019207:beta Carotene