The protein quality control system manages plant defence compound synthesis.

Jacob Pollier, Tessa Moses, Miguel González-Guzmán, Nathan De Geyter, Saskia Lippens, Robin Vanden Bossche, Peter Marhavý, Anna Kremer, Kris Morreel, Christopher J Guérin, Aldo Tava, Wieslaw Oleszek, Johan M Thevelein, Narciso Campos, S Goormachtig, Alain Goossens

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 attackers1,2,3. Knowledge of the conserved jasmonate perception and early signalling machineries is increasing3,4,5,6, 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 sterols7,8,9. 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 HMGR10,11,12,13. 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.
Original languageEnglish
Pages (from-to)148-152
Number of pages5
Publication statusPublished - 10 Nov 2013


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