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

Takahashi, Kaori; Takabayashi, Akira; Tanaka, Ayumi; Tanaka, Ryouichi

doi:10.1074/jbc.m113.525428

Cited by 43 publications

(49 citation statements)

References 42 publications

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“…It is particularly noteworthy that Pchlide, a substrate for its binding partner POR, binds to LIL3 with a higher affinity than any other tetrapyrrole tested. The K D values of LIL3 for metabolites of Chl synthesis are in agreement with previous values reported by Mork-Jansson et al (2015b), while Takahashi et al (2014) placed more emphasis on the membrane-anchoring function of LIL3 for its interacting protein partner. Further specific binding properties of LIL3 for tetrapyrroles will be explored in the future, including the identification of the specific amino acid residues involved.…”

Section: Lil3 and Its Tetrapyrrole-binding Propertysupporting

confidence: 81%

“…Based on these data, we conclude that the stability of CHLP and POR depends on LIL3 expression and that its interaction with these proteins mediates their selective localization at the plastid membranes. These results also are consistent with the stabilization of transgenic CHLP variants, which were supplemented with the transmembrane domain of LIL3 (Takahashi et al, 2014). These transformants showed complementation of the lil3.1/lil3.2 double mutant.…”

Section: Lil3 Stabilizes Porsupporting

confidence: 76%

“…In this context, it is interesting that the expression of the CHLP protein supplemented with the transmembrane domain of either LIL3 or ascorbate peroxidase is sufficient to anchor and stabilize CHLP in the absence of LIL3 (Takahashi et al, 2014). The authors concluded that CHLP function could be restored in lil3 mutants, although the oligomeric CHLP complexes observed in the presence of LIL3 might not be rescued.…”

mentioning

confidence: 90%

“…1) is followed by the two transmembrane domains and a hydrophilic C-terminal segment that protrudes into the stroma of the plastid. In previous reports (Tanaka et al, 2010;Takahashi et al, 2014;Mork-Jansson et al, 2015a, 2015b, LIL3 was proposed to serve as a membrane anchor for other proteins and as a binding site for Chl. Specifically, it was proposed that LIL3 contributes to the formation of diverse protein complexes involved in Chl synthesis or to the assembly of Chl into Chl-binding proteins during their integration into the thylakoid membrane and subsequent assembly into photosynthetic protein complexes.…”

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confidence: 99%

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LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis in Arabidopsis thaliana

et al. 2017

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The LIL3 protein of Arabidopsis (Arabidopsis thaliana) belongs to the light-harvesting complex (LHC) protein family, which also includes the light-harvesting chlorophyll-binding proteins of photosystems I and II, the early-light-inducible proteins, PsbS involved in nonphotochemical quenching, and the one-helix proteins and their cyanobacterial homologs designated high-light-inducible proteins. Each member of this family is characterized by one or two LHC transmembrane domains (referred to as the LHC motif) to which potential functions such as chlorophyll binding, protein interaction, and integration of interacting partners into the plastid membranes have been attributed. Initially, LIL3 was shown to interact with geranylgeranyl reductase (CHLP), an enzyme of terpene biosynthesis that supplies the hydrocarbon chain for chlorophyll and tocopherol. Here, we show another function of LIL3 for the stability of protochlorophyllide oxidoreductase (POR). Multiple protein-protein interaction analyses suggest the direct physical interaction of LIL3 with POR but not with chlorophyll synthase. Consistently, LIL3-deficient plants exhibit substantial loss of POR as well as CHLP, which is not due to defective transcription of the POR and CHLP genes but to the posttranslational modification of their protein products. Interestingly, in vitro biochemical analyses provide novel evidence that LIL3 shows high binding affinity to protochlorophyllide, the substrate of POR. Taken together, this study suggests a critical role for LIL3 in the organization of later steps in chlorophyll biosynthesis. We suggest that LIL3 associates with POR and CHLP and thus contributes to the supply of the two metabolites, chlorophyllide and phytyl pyrophosphate, required for the final step in chlorophyll a synthesis.

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Section: Lil3 and Its Tetrapyrrole-binding Propertysupporting

confidence: 81%

Section: Lil3 Stabilizes Porsupporting

confidence: 76%

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confidence: 90%

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confidence: 99%

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LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis in Arabidopsis thaliana

et al. 2017

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“…GGR is anchored to thylakoid membranes by light-harvestinglike protein 3 (LIL3) in Arabidopsis (18)(19)(20). We found only one rice LIL3 ortholog (OsLIL3, Os02g03330).…”

Section: Osggpps1/osgrp Heterodimer Exists In a Multiprotein Complexmentioning

confidence: 91%

A recruiting protein of geranylgeranyl diphosphate synthase controls metabolic flux toward chlorophyll biosynthesis in rice

Zhou

Wang

Gutensohn

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

110

100

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In plants, geranylgeranyl diphosphate (GGPP) is produced by plastidic GGPP synthase (GGPPS) and serves as a precursor for vital metabolic branches, including chlorophyll, carotenoid, and gibberellin biosynthesis. However, molecular mechanisms regulating GGPP allocation among these biosynthetic pathways localized in the same subcellular compartment are largely unknown. We found that rice contains only one functionally active GGPPS, OsGGPPS1, in chloroplasts. A functionally active homodimeric enzyme composed of two OsGGPPS1 subunits is located in the stroma. In thylakoid membranes, however, the GGPPS activity resides in a heterodimeric enzyme composed of one OsGGPPS1 subunit and GGPPS recruiting protein (OsGRP). OsGRP is structurally most similar to members of the geranyl diphosphate synthase small subunit type II subfamily. In contrast to members of this subfamily, OsGRP enhances OsGGPPS1 catalytic efficiency and specificity of GGPP production on interaction with OsGGPPS1. Structural biology and protein interaction analyses demonstrate that affinity between OsGRP and OsGGPPS1 is stronger than between two OsGGPPS1 molecules in homodimers. OsGRP determines OsGGPPS1 suborganellar localization and directs it to a large protein complex in thylakoid membranes, consisting of geranylgeranyl reductase (OsGGR), light-harvesting-like protein 3 (OsLIL3), protochlorophyllide oxidoreductase (OsPORB), and chlorophyll synthase (OsCHLG). Taken together, genetic and biochemical analyses suggest OsGRP functions in recruiting OsGGPPS1 from the stroma toward thylakoid membranes, thus providing a mechanism to control GGPP flux toward chlorophyll biosynthesis.T erpenoids are one of the largest and most structurally diverse classes of plant primary and secondary metabolites and are involved in numerous physiological and ecological processes ranging from growth and development to communication, environmental adaptation, and defense (1, 2). All terpenoids derive from the universal five-carbon (C 5 ) units, isopentenyl diphosphate (IPP) and its allylic isomer dimethylallyl diphosphate (DMAPP), which are synthesized in plants by two compartmentally separated, but metabolically cross-talking, isoprenoid pathways, the mevalonate and methylerythritol phosphate pathways (3). IPP and DMAPP are subsequently used by short-chain prenyltransferases (PTSs) to produce prenyl diphosphate precursors: geranyl diphosphate (GPP, C 10 ), farnesyl diphosphate (FPP, C 15 ), and geranylgeranyl diphosphate (GGPP, C 20 ) (2, 4, 5). Short-chain PTSs determine not only the chain length of their products but also the compartmental localization of product biosynthesis. By catalyzing the branch-point reactions, they control precursor flux toward various classes of terpenoids.Among the prenyl diphosphate intermediates, GGPP biosynthesis represents an essential metabolic node, as this precursor is shared by several vital metabolic pathways, particularly in plastids, including the biosynthesis of carotenoids and their derivatives (e.g., plant hormones abscisic acid and ...

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Transcriptomic Analysis Reveals Suppression of Photosynthesis and Chlorophyll Synthesis Following Gibberellic Acid Treatment on Oil Palm (Elaies guineensis)

Chai

Ooi

et al. 2023

J Plant Growth Regul

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

Cited by 43 publications

References 42 publications

LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis in Arabidopsis thaliana

LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis in Arabidopsis thaliana

A recruiting protein of geranylgeranyl diphosphate synthase controls metabolic flux toward chlorophyll biosynthesis in rice

Transcriptomic Analysis Reveals Suppression of Photosynthesis and Chlorophyll Synthesis Following Gibberellic Acid Treatment on Oil Palm (Elaies guineensis)

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