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Strong light-induced reorganization of pigment-protein complexes of thylakoid membranes in rye (spectroscopic study).
MedLine Citation:
PMID:  22074666     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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 16h daylight photoperiod, photosynthetic photon flux density (PPFD) of 150μmolm(-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 (150μmolm(-2)s(-1)) or high (1200μmolm(-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 734nm). 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:
Ewa Janik; Waldemar Maksymiec; Wojciech Grudziński; Wiesław I Gruszecki
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-8
Journal Detail:
Title:  Journal of plant physiology     Volume:  -     ISSN:  1618-1328     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882059     Medline TA:  J Plant Physiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011 Elsevier GmbH. All rights reserved.
Affiliation:
Department of Plant Physiology, Institute of Biology, Maria Curie-Skłodowska University, Akademicka 19, 20-033 Lublin, Poland.
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