Wax Crystal-Sparse Leaf1 encodes a β–ketoacyl CoA synthase involved in biosynthesis of cuticular waxes on rice leaf

Yu, Dongmei; Ranathunge, Kosala; Hong, Huang; Pei, Zhibin; Franke, Rochus; Schreiber, Lukas; He, Chaozu

doi:10.1007/s00425-008-0770-9

Cited by 88 publications

(66 citation statements)

References 52 publications

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“…S1 d-g). The mutant was designated wsl2 (wax crystal-sparse leaf2), following the previously identified wax crystal-sparse leaf mutant wsl1 (Yu et al 2008).…”

Section: Resultsmentioning

confidence: 99%

Wax crystal-sparse leaf2, a rice homologue of WAX2/GL1, is involved in synthesis of leaf cuticular wax

Mao

Cheng

Lei

et al. 2011

Planta

108

104

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Epicuticular wax in plants limits non-stomatal water loss, inhibits postgenital organ fusion, protects plants against damage from UV radiation and imposes a physical barrier against pathogen infection. Here, we give a detailed description of the genetic, physiological and morphological consequences of a mutation in the rice gene WSL2, based on a comparison between the wild-type and an EMS mutant. The mutant's leaf cuticle membrane is thicker and less organized than that of the wild type, and its total wax content is diminished by ~80%. The mutant is also more sensitive to drought stress. WSL2 was isolated by positional cloning, and was shown to encode a homologue of the Arabidopsis thaliana genes CER3/WAX2/YRE/FLP1 and the maize gene GL1. It is expressed throughout the plant, except in the root. A transient assay carried out in both A. thaliana and rice protoplasts showed that the gene product is deposited in the endoplasmic reticulum. An analysis of the overall composition of the wax revealed that the mutant produces a substantially reduced quantity of C22-C32 fatty acids, which suggests that the function of WSL2 is associated with the elongation of very long-chain fatty acids.

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“…S1 d-g). The mutant was designated wsl2 (wax crystal-sparse leaf2), following the previously identified wax crystal-sparse leaf mutant wsl1 (Yu et al 2008).…”

Section: Resultsmentioning

confidence: 99%

Wax crystal-sparse leaf2, a rice homologue of WAX2/GL1, is involved in synthesis of leaf cuticular wax

Mao

Cheng

Lei

et al. 2011

Planta

108

104

View full text Add to dashboard Cite

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“…WSL1, encoding a rate-limiting enzyme in the FA elongation multienzyme complex for the synthesis of VLCFAs (C20:0-C34:0) from LCFAs (C16:0/C18:0), was significantly suppressed in the dwa1 mutant. Loss of function of WSL1 led to reduced wax load, sparse wax crystals on the leaf cuticle, and a decrease in the levels of VLCFA precursors (17). The drought induction of LACS7 and LACS8, encoding LACSs for activation of free FAs with different chain lengths, was also suppressed in dwa1.…”

Section: Dwa1 Encodes a Megaenzyme-like Protein Highly Conserved Inmentioning

confidence: 98%

“…A wax deposition defect was also found in the leaf cuticle of the GL1-2 and GL1-1/WSL2 mutants (15,16). Additionally, a mutation in a putative ketoacyl CoA synthase [wax crystal-sparse leaf1 (WSL1)] resulted in reduced wax load and crystals on mutant leaves (17).…”

mentioning

confidence: 99%

Putative megaenzyme DWA1 plays essential roles in drought resistance by regulating stress-induced wax deposition in rice

Zhu

Xiong

2013

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

116

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Drought stress is a major limiting factor for crop production. Cuticular wax plays an important role in preventing water loss from drought stress. However, the genetic control of cuticular wax deposition under drought stress conditions has not been characterized. Here, we identified a rice gene Drought-Induced Wax Accumulation 1 (DWA1) encoding a very large protein (2,391 aa in length) containing multiple enzymatic structures, including an oxidoreductase-like domain; a prokaryotic nonribosomal peptide synthetase-like module, including an AMP-binding domain; and an allene oxide synthase-like domain. This previously unreported putative megaenzyme is conserved in vascular plants. A dwa1 KO mutant was highly sensitive to drought stress relative to the WT. DWA1 was preferentially expressed in vascular tissues and epidermal layers and strongly induced by drought stress. The dwa1 mutant was impaired in cuticular wax accumulation under drought stress, which significantly altered the cuticular wax composition of the plant, resulting in increased drought sensitivity. The mutant had reduced levels of very-long-chain fatty acids, and plants overexpressing DWA1 showed elevated levels of very-long-chain fatty acids relative to the WT. The expression of many wax-related genes was significantly suppressed in dwa1 under drought conditions. The AMP-binding domain exhibited in vitro enzymatic activity in activating long-chain fatty acids to form acyl-CoA. Our results suggest that DWA1 controls drought resistance by regulating drought-induced cuticular wax deposition in rice. This finding may have significant implications for improving the drought resistance of crop varieties.abiotic stress | NRPS | Oryza sativa

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“…Among them, FAE1, CER6, and KCS2/DAISY have been shown to be the major enzymes associated with VLCFA biosynthesis for Brassica spp. seed oil, cuticular wax, and aliphatic suberin synthesis, respectively (James et al, 1995;Millar et al, 1999;Todd et al, 1999;Yephremov et al, 1999;Fiebig et al, 2000;Hooker et al, 2002;Yu et al, 2008;Franke et al, 2009;Lee et al, 2009). KCS2/ DAISY and KCS20 are functionally redundant in cuticular wax and root suberin biosynthesis (Lee et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Arabidopsis 3-Ketoacyl-Coenzyme A Synthase9 Is Involved in the Synthesis of Tetracosanoic Acids as Precursors of Cuticular Waxes, Suberins, Sphingolipids, and Phospholipids

et al. 2013

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Very-long-chain fatty acids (VLCFAs) with chain lengths from 20 to 34 carbons are involved in diverse biological functions such as membrane constituents, a surface barrier, and seed storage compounds. The first step in VLCFA biosynthesis is the condensation of two carbons to an acyl-coenzyme A, which is catalyzed by 3-ketoacyl-coenzyme A synthase (KCS). In this study, amino acid sequence homology and the messenger RNA expression patterns of 21 Arabidopsis (Arabidopsis thaliana) KCSs were compared. The in planta role of the KCS9 gene, showing higher expression in stem epidermal peels than in stems, was further investigated. The KCS9 gene was ubiquitously expressed in various organs and tissues, including roots, leaves, and stems, including epidermis, silique walls, sepals, the upper portion of the styles, and seed coats, but not in developing embryos. The fluorescent signals of the KCS9::enhanced yellow fluorescent protein construct were merged with those of BrFAD2::monomeric red fluorescent protein, which is an endoplasmic reticulum marker in tobacco (Nicotiana benthamiana) epidermal cells. The kcs9 knockout mutants exhibited a significant reduction in C24 VLCFAs but an accumulation of C20 and C22 VLCFAs in the analysis of membrane and surface lipids. The mutant phenotypes were rescued by the expression of KCS9 under the control of the cauliflower mosaic virus 35S promoter. Taken together, these data demonstrate that KCS9 is involved in the elongation of C22 to C24 fatty acids, which are essential precursors for the biosynthesis of cuticular waxes, aliphatic suberins, and membrane lipids, including sphingolipids and phospholipids. Finally, possible roles of unidentified KCSs are discussed by combining genetic study results and gene expression data from multiple Arabidopsis KCSs.

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Wax Crystal-Sparse Leaf1 encodes a β–ketoacyl CoA synthase involved in biosynthesis of cuticular waxes on rice leaf

Cited by 88 publications

References 52 publications

Wax crystal-sparse leaf2, a rice homologue of WAX2/GL1, is involved in synthesis of leaf cuticular wax

Wax crystal-sparse leaf2, a rice homologue of WAX2/GL1, is involved in synthesis of leaf cuticular wax

Putative megaenzyme DWA1 plays essential roles in drought resistance by regulating stress-induced wax deposition in rice

Arabidopsis 3-Ketoacyl-Coenzyme A Synthase9 Is Involved in the Synthesis of Tetracosanoic Acids as Precursors of Cuticular Waxes, Suberins, Sphingolipids, and Phospholipids

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