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The protein quality control system manages plant defence compound synthesis

Jacob Pollier (UGent) , Tessa Moses (UGent) , Miguel Gonzalez Guzman (UGent) , Nathan De Geyter (UGent) , Saskia Lippens (UGent) , Robin Vanden Bossche (UGent) , Peter Marhavy (UGent) , Anna Kremer (UGent) , Kris Morreel (UGent) , Chris Guerin (UGent) , et al.
(2013) NATURE. 504(7478). p.148-152
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Abstract
Jasmonates are ubiquitous oxylipin-derived phytohormones that are essential in the regulation of many development, growth and defence processes. Across the plant kingdom, jasmonates act as elicitors of the production of bioactive secondary metabolites that serve in defence against attackers(1-3). Knowledge of the conserved jasmonate perception and early signalling machineries is increasing(3-6), but the downstream mechanisms that regulate defence metabolism remain largely unknown. Here we show that, in the legume Medicago truncatula, jasmonate recruits the endoplasmic-reticulum-associated degradation (ERAD) quality control system to manage the production of triterpene saponins, widespread bioactive compounds that share a biogenic origin with sterols(7-9). An ERAD-type RING membrane-anchor E3 ubiquitin ligase is co-expressed with saponin synthesis enzymes to control the activity of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR), the rate-limiting enzyme in the supply of the ubiquitous terpene precursor isopentenyl diphosphate. Thus, unrestrained bioactive saponin accumulation is prevented and plant development and integrity secured. This control apparatus is equivalent to the ERAD system that regulates sterol synthesis in yeasts and mammals but that uses distinct E3 ubiquitin ligases, of the HMGR degradation 1 (HRD1) type, to direct destruction of HMGR(10-13). Hence, the general principles for the management of sterol and triterpene saponin biosynthesis are conserved across eukaryotes but can be controlled by divergent regulatory cues.
Keywords
MEDICAGO-TRUNCATULA, HMG-COA REDUCTASE, 3-HYDROXY-3-METHYLGLUTARYL-COA REDUCTASE, ENDOPLASMIC-RETICULUM, IDENTIFICATION, YEAST, SAPONIN BIOSYNTHESIS, DEGRADATION, MASS-SPECTROMETRY, TRITERPENOID GLYCOSIDES

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Citation

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MLA
Pollier, Jacob, et al. “The Protein Quality Control System Manages Plant Defence Compound Synthesis.” NATURE, vol. 504, no. 7478, 2013, pp. 148–52, doi:10.1038/nature12685.
APA
Pollier, J., Moses, T., Gonzalez Guzman, M., De Geyter, N., Lippens, S., Vanden Bossche, R., … Goossens, A. (2013). The protein quality control system manages plant defence compound synthesis. NATURE, 504(7478), 148–152. https://doi.org/10.1038/nature12685
Chicago author-date
Pollier, Jacob, Tessa Moses, Miguel Gonzalez Guzman, Nathan De Geyter, Saskia Lippens, Robin Vanden Bossche, Peter Marhavy, et al. 2013. “The Protein Quality Control System Manages Plant Defence Compound Synthesis.” NATURE 504 (7478): 148–52. https://doi.org/10.1038/nature12685.
Chicago author-date (all authors)
Pollier, Jacob, Tessa Moses, Miguel Gonzalez Guzman, Nathan De Geyter, Saskia Lippens, Robin Vanden Bossche, Peter Marhavy, Anna Kremer, Kris Morreel, Chris Guerin, Aldo Tava, Wieslaw Oleszek, Johan M Thevelein, Narciso Campos, Sofie Goormachtig, and Alain Goossens. 2013. “The Protein Quality Control System Manages Plant Defence Compound Synthesis.” NATURE 504 (7478): 148–152. doi:10.1038/nature12685.
Vancouver
1.
Pollier J, Moses T, Gonzalez Guzman M, De Geyter N, Lippens S, Vanden Bossche R, et al. The protein quality control system manages plant defence compound synthesis. NATURE. 2013;504(7478):148–52.
IEEE
[1]
J. Pollier et al., “The protein quality control system manages plant defence compound synthesis,” NATURE, vol. 504, no. 7478, pp. 148–152, 2013.
@article{4224303,
  abstract     = {{Jasmonates are ubiquitous oxylipin-derived phytohormones that are essential in the regulation of many development, growth and defence processes. Across the plant kingdom, jasmonates act as elicitors of the production of bioactive secondary metabolites that serve in defence against attackers(1-3). Knowledge of the conserved jasmonate perception and early signalling machineries is increasing(3-6), but the downstream mechanisms that regulate defence metabolism remain largely unknown. Here we show that, in the legume Medicago truncatula, jasmonate recruits the endoplasmic-reticulum-associated degradation (ERAD) quality control system to manage the production of triterpene saponins, widespread bioactive compounds that share a biogenic origin with sterols(7-9). An ERAD-type RING membrane-anchor E3 ubiquitin ligase is co-expressed with saponin synthesis enzymes to control the activity of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR), the rate-limiting enzyme in the supply of the ubiquitous terpene precursor isopentenyl diphosphate. Thus, unrestrained bioactive saponin accumulation is prevented and plant development and integrity secured. This control apparatus is equivalent to the ERAD system that regulates sterol synthesis in yeasts and mammals but that uses distinct E3 ubiquitin ligases, of the HMGR degradation 1 (HRD1) type, to direct destruction of HMGR(10-13). Hence, the general principles for the management of sterol and triterpene saponin biosynthesis are conserved across eukaryotes but can be controlled by divergent regulatory cues.}},
  author       = {{Pollier, Jacob and Moses, Tessa and Gonzalez Guzman, Miguel and De Geyter, Nathan and Lippens, Saskia and Vanden Bossche, Robin and Marhavy, Peter and Kremer, Anna and Morreel, Kris and Guerin, Chris and Tava, Aldo and Oleszek, Wieslaw and Thevelein, Johan M and Campos, Narciso and Goormachtig, Sofie and Goossens, Alain}},
  issn         = {{0028-0836}},
  journal      = {{NATURE}},
  keywords     = {{MEDICAGO-TRUNCATULA,HMG-COA REDUCTASE,3-HYDROXY-3-METHYLGLUTARYL-COA REDUCTASE,ENDOPLASMIC-RETICULUM,IDENTIFICATION,YEAST,SAPONIN BIOSYNTHESIS,DEGRADATION,MASS-SPECTROMETRY,TRITERPENOID GLYCOSIDES}},
  language     = {{eng}},
  number       = {{7478}},
  pages        = {{148--152}},
  title        = {{The protein quality control system manages plant defence compound synthesis}},
  url          = {{http://doi.org/10.1038/nature12685}},
  volume       = {{504}},
  year         = {{2013}},
}
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