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Functional Analysis of Light-harvesting-like Protein 3 (LIL3) and Its Light-harvesting Chlorophyll-binding Motif in Arabidopsis

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/55188

Title: Functional Analysis of Light-harvesting-like Protein 3 (LIL3) and Its Light-harvesting Chlorophyll-binding Motif in Arabidopsis
Authors: Takahashi, Kaori Browse this author
Takabayashi, Atsushi Browse this author →KAKEN DB
Tanaka, Ayumi Browse this author →KAKEN DB
Tanaka, Ryouichi Browse this author →KAKEN DB
Keywords: chloroplast
light-harvesting-like protein
isoprenyl metabolism
Issue Date: 10-Jan-2014
Publisher: American Society for Biochemistry and Molecular Biology
Journal Title: Journal of biological chemistry
Volume: 289
Issue: 2
Start Page: 987
End Page: 999
Publisher DOI: 10.1074/jbc.M113.525428
Abstract: The light-harvesting complex (LHC) constitutes the major light-harvesting antenna of photosynthetic eukaryotes. LHC contains a characteristic sequence motif, termed LHC motif, consisting of 25-30 mostly hydrophobic amino acids. This motif is shared by a number of transmembrane proteins from oxygenic photoautotrophs that are termed light-harvesting-like (LIL) proteins. To gain insights into the functions of LIL proteins and their LHC motifs, we functionally characterized a plant LIL protein, LIL3. This protein has been shown previously to stabilize geranylgeranyl reductase (GGR), a key enzyme in phytol biosynthesis. It is hypothesized that LIL3 functions to anchor GGR to membranes. First, we conjugated the transmembrane domain of LIL3 or that of ascorbate peroxidase to GGR and expressed these chimeric proteins in an Arabidopsis mutant lacking LIL3 protein. As a result, the transgenic plants restored phytol-synthesizing activity. These results indicate that GGR is active as long as it is anchored to membranes, even in the absence of LIL3. Subsequently, we addressed the question why the LHC motif is conserved in the LIL3 sequences. We modified the transmembrane domain of LIL3, which contains the LHC motif, by substituting its conserved amino acids (Glu-171, Asn-174, and Asp-189) with alanine. As a result, the Arabidopsis transgenic plants partly recovered the phytol-biosynthesizing activity. However, in these transgenic plants, the LIL3-GGR complexes were partially dissociated. Collectively, these results indicate that the LHC motif of LIL3 is involved in the complex formation of LIL3 and GGR, which might contribute to the GGR reaction.
Rights: This research was originally published in Journal of Biological Chemistry. Takahashi Kaori, Takabayashi Atsushi, Tanaka Ayumi, and Tanaka Ryouichi. Functional Analysis of Light-harvesting-like Protein 3 (LIL3) and Its Light-harvesting Chlorophyll-binding Motif in Arabidopsis. Journal of biological chemistry. 2014; Vol289(2): pp987-999. © the American Society for Biochemistry and Molecular Biology.
Type: article (author version)
URI: http://hdl.handle.net/2115/55188
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: 田中 亮一

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