ArticleThe Journal of biological chemistry2014
Functional analysis of light-harvesting-like protein 3 (LIL3) and its light-harvesting chlorophyll-binding motif in Arabidopsis.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 56 citations in OpenAlex.
- De novo coassembly of functional chlorophyll- and carotenoid-protein complexes inScience advances · 2026Article
- Phytol in Skin Care: From Multidimensional Pharmacological Mechanisms to Nanocarrier-Based Cosmetic Applications.International journal of molecular sciences · 2026Review
- Quantitative western blotting adapted for expanded sample capacity with non-linear curve fitting.Journal of plant research · 2026Article
- TkSRPP3/4 interactors TkGGR1 and TkLIL3 link plastid-like organelles with isoprenoid metabolism in Taraxacum koksaghyz latex.Plant cell reports · 2025Article
- Article
- Whole-Transcriptome Sequencing Reveals a ceRNA Regulatory Network Associated with the Process of Periodic Albinism under Low Temperature in Baiye No. 1 (International journal of molecular sciences · 2023Article
- Verification of the Relationship between Redox Regulation of Thioredoxin Target Proteins and Their Proximity to Thylakoid Membranes.Antioxidants (Basel, Switzerland) · 2022Article
- Plant LHC-like proteins show robust folding and static non-photochemical quenching.Nature communications · 2021Article
- Accumulation of geranylgeranylated chlorophylls in the pigment-protein complexes of Arabidopsis thaliana acclimated to green light: effects on the organization of light-harvesting complex II and photosystem II functions.Photosynthesis research · 2021Article
- Light Harvesting in Fluctuating Environments: Evolution and Function of Antenna Proteins across Photosynthetic Lineage.Plants (Basel, Switzerland) · 2021Article
- Light Harvesting-like Protein 3 Interacts with Phytoene Synthase and Is Necessary for Carotenoid and Chlorophyll Biosynthesis in Rice.Rice (New York, N.Y.) · 2021Article
- ONE-HELIX PROTEIN1 and 2 Form Heterodimers to Bind Chlorophyll in Photosystem II Biogenesis.Plant physiology · 2020Article
- A lil3 chlp double mutant with exclusive accumulation of geranylgeranyl chlorophyll displays a lethal phenotype in rice.BMC plant biology · 2019Article
- The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration.The Journal of biological chemistry · 2019Article
- A strategy to characterize chlorophyll protein interaction in LIL3.Plant methods · 2019Article
- Stable Accumulation of Photosystem II Requires ONE-HELIX PROTEIN1 (OHP1) of the Light Harvesting-Like Family.Plant physiology · 2018Article
- Characterization of chlorophyll binding to LIL3.PloS one · 2018Article
- A recruiting protein of geranylgeranyl diphosphate synthase controls metabolic flux toward chlorophyll biosynthesis in rice.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis inPlant physiology · 2017Article
- Metabolic Origins and Transport of Vitamin E Biosynthetic Precursors.Frontiers in plant science · 2017Review
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4 authors at 1 institution in 1 country.
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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.
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