Heat shock protein 90 co-chaperone modules fine-tune the antagonistic interaction between salicylic acid and auxin biosynthesis in cassava.
Heat shock protein 90 co-chaperone modules fine-tune the antagonistic interaction between salicylic acid and auxin biosynthesis in cassava.
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DOI:
10.1016/j.celrep.2021.108717
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发表时间:
2021-02
期刊:
影响因子:
8.8
通讯作者:
Yunxie Wei;Binbin Zhu;Wen Liu;Xiao Cheng;Daozhe Lin;Chaozu He;Haitao Shi
中科院分区:
文献类型:
--
作者:
Yunxie Wei;Binbin Zhu;Wen Liu;Xiao Cheng;Daozhe Lin;Chaozu He;Haitao Shi
Heat shock protein 90 (HSP90) is an important molecular chaperone in plants. However, HSP90-mediated plant immune response remains elusive in cassava. In this study, cassava bacterial blight (CBB) induces the expression ofMeHsf8, which directly targetsMeHSP90.9to activate its expression and immune response. Further identification of SHI-related sequence 1 (MeSRS1) and MeWRKY20 as MeHSP90.9 co-chaperones revealed the underlying mechanism of MeHSP90.9-mediated immune response. MeHSP90.9 interacts with MeSRS1 and MeWRKY20 to promote their transcriptional activation of salicylic acid (SA) biosynthetic geneavrPphB Susceptible 3(MePBS3) and tryptophan metabolic geneN-acetylserotonin O-methyltransferase 2(MeASMT2), respectively, so as to activate SA biosynthesis but inhibit tryptophan-derived auxin biosynthesis. Notably, genetic experiments confirmed that overexpressingMePBS3andMeASMT2could rescue the effects of silencing MeHsf8-MeHSP90.9 on disease resistance. This study highlights the dual regulation of SA and auxin biosynthesis by MeHSP90.9, providing the mechanistic understanding of MeHSP90.9 client partners in plant immunity.