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The Oligomeric States of the Photosystems and the Light-Harvesting Complexes in the Chl b-Less Mutant

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/50292

Title: The Oligomeric States of the Photosystems and the Light-Harvesting Complexes in the Chl b-Less Mutant
Authors: Takabayashi, Atsushi Browse this author →KAKEN DB
Kurihara, Katsunori Browse this author
Kuwano, Masayoshi Browse this author
Kasahara, Yasuhiro Browse this author →KAKEN DB
Tanaka, Ryouichi Browse this author →KAKEN DB
Tanaka, Ayumi Browse this author →KAKEN DB
Keywords: Arabidopsis thaliana
Blue-native-PAGE
Chl b-less plant
Photosystem
Issue Date: Dec-2011
Publisher: Oxford University Press
Journal Title: Plant and Cell Physiology
Volume: 52
Issue: 12
Start Page: 2103
End Page: 2114
Publisher DOI: 10.1093/pcp/pcr138
PMID: 22006940
Abstract: The reversible associations between the light-harvesting complexes (LHCs) and the core complexes of PSI and PSII are essential for the photoacclimation mechanisms in higher plants. Two types of chlorophylls, chlorophyll a and chlorophyll b, both function in light harvesting and are required for the biogenesis of the photosystems. Chlorophyll b-less plants have been studied to determine the function of the LHCs because the chlorophyll b deficiency has severe effects specific to the LHCs. Previous studies have shown that the amounts of the LHCs, especially the LHCII trimer, were decreased in the mutants; however, it is still unclear whether chlorophyll b is required for the assembly of the LHCs and for the association of the LHCs with PSI and PSII. Here, to reveal the function of chlorophyll b in the LHCs, we investigated the oligomeric states of the LHCs, PSI and PSII in the Arabidopsis chlorophyll b-less mutant. A two-dimensional blue native-PAGE/SDS-PAGE demonstrated that the PSI-LHCI supercomplex was fully assembled in the absence of chlorophyll b, whereas the trimeric LHCII and PSII-LHCII supercomplexes were not detected. The PSI-NAD(P)H dehydrogenase (NDH) supercomplexes were also assembled in the mutant. Furthermore, we detected two forms of monomeric LHC proteins. The faster migrating forms, which were detected primarily in the mutant, were likely apo-LHC proteins, whereas the slower migrating forms were likely the LHC proteins that contained chlorophyll a. These findings increase our understanding of the chlorophyll b function in the assembly of LHCs and the association of the LHCs with PSI, PSII and NDH.
Rights: This is a pre-copy-editing, author-produced PDF of an article accepted for publication in Plant and Cell Physiology following peer review. The definitive publisher-authenticated version Plant Cell Physiol (2011) 52 (12): 2103-2114 is available online at: http://pcp.oxfordjournals.org/content/52/12/2103
Type: article (author version)
URI: http://hdl.handle.net/2115/50292
Appears in Collections:低温科学研究所 (Institute of Low Temperature Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 高林 厚史

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