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Chalcone synthase is ubiquitinated and degraded via interactions with a RING-H2 protein in petals of Paeonia 'He Xie'

文献类型：期刊论文

作者Gu, Zhaoyu; Men, Siqi2; Zhu, Jin2; Hao, Qing4; Tong, Ningning2; Liu, Zheng-An; Zhang, Hechen1; Shu, Qingyan; Wang, Liangsheng2
刊名JOURNAL OF EXPERIMENTAL BOTANY
出版日期2019
卷号70期号:18页码:4749-4762
关键词Chalcone synthase degradation flavonoid biosynthesis Paeonia RING-H2 ubiquitination
ISSN号0022-0957
DOI10.1093/jxb/erz245
文献子类Article
英文摘要Flavonoids are secondary metabolites widely distributed among angiosperms, where they play diverse roles in plant growth, development, and evolution. The regulation of flavonoid biosynthesis in plants has been extensively studied at the transcriptional level, but post-transcriptional, translational, and post-translational control of flavonoid biosynthesis remain poorly understood. In this study, we analysed post-translational regulation of flavonoid biosynthesis in the ornamental plant Paeonia, using proteome and ubiquitylome profiling, in conjunction with transcriptome data. Three enzymes involved in flavonoid biosynthesis were identified as being putative targets of ubiquitin-mediated degradation. Among these, chalcone synthase (PhCHS) was shown to have the greatest number of ubiquitination sites. We examined PhCHS abundance in petals using PhCHS-specific antibody and found that its accumulation decreased at later developmental stages, resulting from 26S proteasome-mediated degradation. We further identified a ring domain-containing protein (PhRING-H2) that physically interacts with PhCHS and demonstrated that PhRING-H2 is required for PhCHS ubiquitination. Taken together, our results suggest that PhRING-H2-mediates PhCHS ubiquitination and degradation is an important mechanism of post-translational regulation of flavonoid biosynthesis in Paeonia, providing a theoretical basis for the manipulation of flavonoid biosynthesis in plants.
学科主题Plant Sciences
出版地OXFORD
电子版国际标准刊号1460-2431
WOS关键词FLAVONOID BIOSYNTHESIS ; ANTHOCYANIN ACCUMULATION ; FLOWER COLORATION ; COLORFUL MODEL ; E3 LIGASE ; DEGRADATION ; PATHWAY ; GENE ; TOLERANCE ; REGULATOR
WOS研究方向Plant Sciences
语种英语
WOS记录号WOS:000493107700015
出版者OXFORD UNIV PRESS
资助机构National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31471909, 31772350]
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/19617]  
专题中科院北方资源植物重点实验室
作者单位1.Qingdao Agr Univ, Coll Landscape Architecture & Forestry, Qingdao 266109, Shandong, Peoples R China
2.Chinese Acad Sci, Key Lab Plant Resources, Beijing Bot Garden, Inst Bot, Beijing 100093, Peoples R China
3.Henan Acad Agr Sci, Inst Hort, Zhengzhou 450002, Henan, Peoples R China
4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714		 Gu, Zhaoyu,Men, Siqi,Zhu, Jin,et al. Chalcone synthase is ubiquitinated and degraded via interactions with a RING-H2 protein in petals of Paeonia 'He Xie'[J]. JOURNAL OF EXPERIMENTAL BOTANY,2019,70(18):4749-4762.
APA Gu, Zhaoyu.,Men, Siqi.,Zhu, Jin.,Hao, Qing.,Tong, Ningning.,...&Wang, Liangsheng.(2019).Chalcone synthase is ubiquitinated and degraded via interactions with a RING-H2 protein in petals of Paeonia 'He Xie'.JOURNAL OF EXPERIMENTAL BOTANY,70(18),4749-4762.
MLA Gu, Zhaoyu,et al."Chalcone synthase is ubiquitinated and degraded via interactions with a RING-H2 protein in petals of Paeonia 'He Xie'".JOURNAL OF EXPERIMENTAL BOTANY 70.18(2019):4749-4762.

入库方式： OAI收割

来源：植物研究所

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