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A trans-long-chain prenyl diphosphate synthase promotes ubiquinone 10 biosynthesis in grape

文献类型： 外文期刊

作者： Wang, Peipei 1 ; Ren, Tingting 1 ; You, Ruyue 1 ; Cao, Yazheng 3 ; Xu, Yang 3 ; Wei, Guo 3 ; Liu, Yuting 1 ; Ji, Xinglong 1 ; Ren, Yiran 1 ; Zhang, Kekun 4 ; Zhou, Yongfeng 5 ; Sun, Lei 7 ; Leng, Xiangpeng 1 ;

作者机构： 1.Qingdao Agr Univ, Inst Grape Sci & Engn, Coll Hort, Qingdao 266109, Peoples R China

2.Qingdao Agr Univ, Coll Hort, Engn Lab Genet Improvement Hort Crops Shandong Pro, Qingdao 266109, Peoples R China

3.Yangzhou Univ, Coll Hort & Landscape Architecture, Yangzhou 225009, Peoples R China

4.Northwest A&F Univ, Coll Enol, Yangling 712100, Peoples R China

5.Chinese Acad Agr Sci, Agr Genom Inst Shenzhen, Natl Key Lab Trop Crop Breeding, Shenzhen Branch,Guangdong Lab Lingnan Modern Agr,M, Shenzhen 518120, Peoples R China

6.Chinese Acad Trop Agr Sci, Trop Crops Genet Resources Inst, Natl Key Lab Trop Crop Breeding, Haikou 571101, Peoples R China

7.Beijing Acad Agr & Forestry Sci, Inst Forestry & Pomol, Beijing 100093, Peoples R China

期刊名称：PLANT PHYSIOLOGY （ 影响因子：6.9； 五年影响因子：7.7 ）

ISSN： 0032-0889

年卷期： 2025 年 198 卷 3 期

页码：

收录情况： SCI

摘要： Prenyl diphosphate synthase (PDS) plays indispensable roles in terpene biosynthesis. However, there is an ongoing debate regarding whether grape (Vitis vinifera) geranyl diphosphate synthase (VvGDS, VIT_15s0024g00850) can generate geranyl diphosphate (GPP), the precursor of monoterpene biosynthesis. Here, we demonstrated that VvGDS localizes in mitochondria and is an authentic trans-long-chain PDS (thus, VvGDS was renamed VvPDS), which is essential for ubiquinone (UQ) biosynthesis. This finding is in contrast to the initial association of VvPDS with GDS activity related to monoterpene biosynthesis. VvPDS not only falls within the subgroup comprising mitochondrial trans-long-chain PDSs, which participate in UQ biosynthesis in other eukaryotes, but also exhibits a positive association with UQ10 content in different grape tissues. VvPDS cannot catalyze GPP biosynthesis using isopentenyl diphosphate and dimethylallyl diphosphate as substrates. Furthermore, VvPDS functionally complements the yeast coq1 mutation lacking mitochondrial hexaprenyl diphosphate synthase activity and catalyzes UQ10 and UQ9 biosynthesis. Transient overexpression of VvPDS in grape leaves increased UQ10 accumulation, whereas silencing VvPDS caused an obvious reduction in UQ10 content. Similarly, the stable overexpression of VvPDS enhanced UQ10 accumulation in tobacco (Nicotiana tabacum), and these UQ10-overproducing plants exhibited improved oxidative stress tolerance, primarily through enhanced reactive oxygen species-scavenging capacity. Taken together, these findings provide biochemical and genetic evidence supporting UQ biosynthesis in grape and encourage future research to reevaluate the enzymatic functions and physiological roles of angiosperm PDSs. VvPDS is an authentic trans-long-chain prenyl diphosphate synthase and is involved in ubiquinone 10 biosynthesis.

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