J Integr Plant Biol. ›› 2023, Vol. 65 ›› Issue (5): 1170-1182.DOI: 10.1111/jipb.13454

• Metabolism and Biochemistry • Previous Articles     Next Articles

Heteromerization of short‐chain trans‐prenyltransferase controls precursor allocation within a plastidial terpenoid network

Yihua Ma1,2†, Qingwen Chen1†, Yaoyao Wang1,2, Fengxia Zhang1, Chengyuan Wang3 and Guodong Wang1,2,3*   

  1. 1. State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, The Innovative Academy of Seed Design, Chinese Academy of Sciences, Beijing 100101, China;
    2. University of Chinese Academy of Sciences, Beijing 100039, China;
    3. Center for Microbes, Development and Health, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai 200031, China
    Yihua Ma and Qingwen Chen contributed equally to this work.
    *Correspondence: Guodong Wang (gdwang@genetics.ac.cn)
  • Received:2022-09-19 Accepted:2023-01-16 Online:2023-03-15 Published:2023-05-01

Abstract: Terpenes are the largest and most diverse class of plant specialized metabolites. Sesterterpenes (C25), which are derived from the plastid methylerythritol phosphate pathway, were recently characterized in plants. In Arabidopsis thaliana, four genes encoding geranylfarnesyl diphosphate synthase (GFPPS) (AtGFPPS1 to 4) are responsible for the production of GFPP, which is the common precursor for sesterterpene biosynthesis. However, the interplay between sesterterpenes and other known terpenes remain elusive. Here, we first provide genetic evidence to demonstrate that GFPPSs are responsible for sesterterpene production in Arabidopsis. Blockage of the sesterterpene pathway at the GFPPS step increased the production of geranylgeranyl diphosphate (GGPP)-derived terpenes. Interestingly, co-expression of sesterTPSs in GFPPS-OE (overexpression) plants rescued the phenotypic changes of GFPPS-OE plants by restoring the endogenous GGPP. We further demonstrated that, in addition to precursor (DMAPP/IPP) competition by GFPPS and GGPP synthase (GGPPS) in plastids, GFPPS directly decreased the activity of GGPPS through protein-protein interaction, ultimately leading to GGPP deficiency in planta. Our study provides a new regulatory mechanism of the plastidial terpenoid network in plant cells.

Key words: Arabidopsis, geranylfarnesyl diphosphate synthase, geranylgeranyl pyrophosphate synthase, plastid, sesterterpene, terpene network

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