title: Strong light-induced reorganization of pigment-protein complexes of thylakoid membranes in rye (spectroscopic study).
abstract: The supramolecular reorganization of LHCII complexes within the thylakoid membrane in Secale cereale leaves under low and high light condition was examined. Rye seedlings were germinated hydroponically in a climate chamber with a 16 h daylight photoperiod, photosynthetic photon flux density (PPFD) of 150 μmo lm(-2)s(-1) and 24/16°C day/night temperature. The influence of pre-illumination of the plants with high light intensity on the PSII antenna complexes was studied by comparison of the structure and function of the LHCII complexes and organization of thylakoid membranes isolated from 10-day-old plants illuminated with low (150 μmo lm(-2)s(-1)) or high (1200 μmo lm(-2)s(-1)) light intensity. Aggregated and trimeric with monomeric forms of LHCII complexes were separated from the whole thylakoid membranes using non-denaturing electrophoresis. Analyses of fluorescence emission spectra of these different LHCII forms showed that the monomer was the most effective aggregating antenna form. Moreover, photoprotection connected with LHCII aggregation was more effective upon LHCII monomers in comparison to trimer aggregation. Light stress induced specific organization of neighboring LHCII complexes, causing an increase in fluorescence yield of the long-wavelength bands (centered at 701 and 734 nm). The changes in the organization of the thylakoid membrane under light stress, observed by analysis of absorbance spectra obtained by Fourier transform infrared spectroscopy, also indicated light-induced LHCII aggregation.
authors.affiliation: Department of Plant Physiology, Institute of Biology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, Poland. ewa.janik@poczta.umcs.lublin.pl
authors.forename: Ewa
authors.initials: E
authors.lastname: Janik
authors.forename: Waldemar
authors.initials: W
authors.lastname: Maksymiec
authors.forename: Wojciech
authors.initials: W
authors.lastname: Grudziński
authors.forename: Wiesław I
authors.initials: WI
authors.lastname: Gruszecki
mesh_terms: D000222:Adaptation, Physiological; D004586:Electrophoresis; D008027:Light; D045342:Light-Harvesting Protein Complexes / Q000528:radiation effects* / Q000648:ultrastructure; D017440:Photoperiod; D045332:Photosystem II Protein Complex / Q000528:radiation effects / Q000648:ultrastructure; D012434:Secale / Q000502:physiology / Q000528:radiation effects* / Q000648:ultrastructure; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013312:Stress, Physiological; D020524:Thylakoids / Q000000981:diagnostic imaging / Q000528:radiation effects*; D014463:Ultrasonography
chemical_list: D045342:Light-Harvesting Protein Complexes; D045332:Photosystem II Protein Complex