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The Arabidopsis ref2 Mutant Is Defective in the Gene Encoding CYP83A1 and Shows Both Phenylpropanoid and Glucosinolate Phenotypes
Open accessAbstract
The Arabidopsis ref2 mutant was identified in a screen for plants having altered fluorescence under UV light. Characterization of the ref2 mutants showed that they contained reduced levels of a number of phenylpropanoid pathway-derived products: sinapoylmalate in leaves, sinapoylcholine in seeds, and syringyl lignin in stems. Surprisingly, positional cloning of the REF2 locus revealed that it encodes CYP83A1, a cytochrome P450 sharing a high degree of similarity to CYP83B1, an enzyme involved in glucosinolate biosynthesis. Upon further investigation, ref2 mutants were found to have reduced levels of all aliphatic glucosinolates and increased levels of indole-derived glucosinolates in their leaves. These results show that CYP83A1 is involved in the biosynthesis of both short-chain and long-chain aliphatic glucosinolates and suggest a novel metabolic link between glucosinolate biosynthesis, a secondary biosynthetic pathway found only in plants in the order Capparales, and phenylpropanoid metabolism, a pathway found in all plants and considered essential to the survival of terrestrial plant species.
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Glucosinolates and benzoxazinoids also seem to regulate the accumulation of other secondary metabolites.
“Interestingly, glucosinolates and benzoxazinoids also seem to regulate the accumulation of other secondary metabolites (Hemm et al., 2003;Kim et al., 2015;Li et al., 2018a).”
From Plant Secondary Metabolites as Defenses, Regulators, and Primary Metabolites: The Blurred Functional Trichotomy (2020) · cites this paper as Hemm et al., 2003
The section “Phenylpropanoid Biosynthesis Is Altered in ref2” (page unavailable) links a defect in glucosinolate biosynthesis to altered phenylpropanoid metabolism in Arabidopsis, possibly through accumulated aldoximes. This supports a connection between the pathways, but does not show that glucosinolates themselves regulate other metabolites. The paper does not address benzoxazinoids. (LLM, conf=0.83)
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Research works printed but not linked: 8
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- Chapple, C.C.S., Shirley, B.W., Zook, M., Hammerschmidt, R., and Somerville, S.C. (1994). Secondary metabolism in Arabidop- sis. In Arabidopsis, E.M. Meyerowitz and C.R. Somerville, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), pp. 989-1030.
- Hull, A.K., Vij, R., and Celenza, J.L. (2000). Arabidopsis cyto- chrome P450s that catalyze the first step of tryptophan-depen- dent indole-3-acetic acid biosynthesis. Proc. Natl. Acad. Sci. USA 97, 2379-2384.
- Humphreys, J.M., Hemm, M.R., and Chapple, C. (1999). New routes for lignin biosynthesis defined by biochemical character- ization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 96, 10045-10050.
- Meyer, K., Benning, G., and Grill, E. (1996). Cloning of plant genes based on genetic map location. In Genome Mapping in Plants, A.H. Paterson, ed (New York: Academic Press/Austin, TX: Landes Bioscience Publishers), pp. 137-154.
- Meyer, K., Shirley, A.M., Cusumano, J.C., Bell-Lelong, D.A., and Chapple, C. (1998). Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxyge- nase in Arabidopsis. Proc. Natl. Acad. Sci. USA 95, 6619-6623.
- Osakabe, K., Tsao, C.C., Li, L.G., Popko, J.L., Umezawa, T., Carraway, D.T., Smetzer, R.H., Joshi, C.P., and Chiang, V.L. (1999). Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms. Proc. Natl. Acad. Sci. USA 96, 8955-8960.
- Siminszky, B., Corbin, F.T., Ward, E.R., Fleischmann, T.J., and Dewey, R.E. (1999). Expression of a soybean cytochrome P450 monooxygenase cDNA in yeast and tobacco enhances the metab- olism of phenylurea herbicides. Proc. Natl. Acad. Sci. USA 96, 1750-1755.
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Erb, M., & Kliebenstein, D. J. (2020) · Plant Physiology · doi:10.1104/pp.20.00433 · Cited by 1,333
Metadata
- Authors
- Hemm, M. R., Ruegger, M. O., & Chapple, C.
- Affiliations
- Purdue University West Lafayette (US)
- Venue
- The Plant Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-12-19
- Volume
- 15
- Issue
- 1
- Pages
- 179-194
- ISSN
- 1040-4651 (ISSN-L)
- 1532-298X
- PMC
- PMC143490
- OpenAlex
- W1972020725
- Cited by
- 198
- References
- 0
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 3 · 2023: 8 · 2022: 5 · 2021: 10 · 2020: 14 · 2019: 11 · 2018: 5 · 2017: 9 · 2016: 8 · 2015: 6 · 2014: 11 · 2013: 6 · 2012: 12
- FWCI
- 2.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Plant Cell (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- U.S. Department of Energy
- Purdue University
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant Gene Expression Analysis
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- cytochrome P450, glucosinolate biosynthesis, phenylpropanoid metabolism, syringyl lignin, aliphatic glucosinolates, indole glucosinolates, UV fluorescence, positional cloning
- MeSH terms
- Chromosome Mapping, Cloning, Molecular, Cytochrome P-450 Enzyme System, Glucosinolates, Mixed Function Oxygenases, Lignin, Malates, Methylation, Methyltransferases, Mutation, Oximes, Phenotype, Phenylpropionates, Plant Extracts, Seeds, Arabidopsis, Plant Leaves, Plant Stems, Chromosomes, Artificial, Bacterial, Arabidopsis Proteins
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