The SmMYC2–SmMYB36 complex is involved in methyl jasmonate‐mediated tanshinones biosynthesis in Salvia miltiorrhiza

Author:

Cao Ruizhi1,Lv Bingbing1,Shao Shuai1,Zhao Ying1,Yang Mengdan1,Zuo Anqi1,Wei Jia2,Dong Juane1ORCID,Ma Pengda1ORCID

Affiliation:

1. College of Life Sciences Northwest A&F University Yangling 712100 China

2. Jilin Provincial Key Laboratory of Agricultural Biotechnology Jilin Academy of Agricultural Sciences (Northeast Agricultural Research Center of China) Changchun 130033 China

Abstract

SUMMARYThe jasmonic acid (JA) signaling pathway plays an important role in promoting the biosynthesis of tanshinones. While individual transcription factors have been extensively studied in the context of tanshinones biosynthesis regulation, the influence of methyl jasmonate (MeJA)‐induced transcriptional complexes remains unexplored. This study elucidates the positive regulatory role of the basic helix–loop–helix protein SmMYC2 in tanshinones biosynthesis in Salvia miltiorrhiza. SmMYC2 not only binds to SmGGPPS1 promoters, activating their transcription, but also interacts with SmMYB36. This interaction enhances the transcriptional activity of SmMYC2 on SmGGPPS1, thereby promoting tanshinones biosynthesis. Furthermore, we identified three JA signaling repressors, SmJAZ3, SmJAZ4, and SmJAZ8, which interact with SmMYC2. These repressors hindered the transcriptional activity of SmMYC2 on SmGGPPS1 and disrupted the interaction between SmMYC2 and SmMYB36. MeJA treatment triggered the degradation of SmJAZ3 and SmJAZ4, allowing the SmMYC2–SmMYB36 complex to subsequently activate the expression of SmGGPPS1, whereas SmJAZ8 inhibited MeJA‐mediated degradation due to the absence of the LPIARR motif. These results demonstrate that the SmJAZ‐SmMYC2–SmMYB36 module dynamically regulates the JA‐mediated accumulation of tanshinones. Our results reveal a new regulatory network for the biosynthesis of tanshinones. This study provides valuable insight for future research on MeJA‐mediated modulation of tanshinones biosynthesis.

Funder

National Natural Science Foundation of China

Publisher

Wiley

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