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Chalcone synthase is ubiquitinated and degraded via interactions with a RING-H2 protein in petals of Paeonia 'He Xie' | |
Gu, Zhaoyu; Men, Siqi1; Zhu, Jin1; Hao, Qing2; Tong, Ningning1; Liu, Zheng-An![]() ![]() | |
2019 | |
Source Publication | JOURNAL OF EXPERIMENTAL BOTANY
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ISSN | 0022-0957 |
Volume | 70Issue:18Pages:4749-4762 |
Abstract | 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. |
Keyword | Chalcone synthase degradation flavonoid biosynthesis Paeonia RING-H2 ubiquitination |
Subject Area | Plant Sciences |
DOI | 10.1093/jxb/erz245 |
Indexed By | SCI |
Language | 英语 |
WOS Keyword | FLAVONOID BIOSYNTHESIS ; ANTHOCYANIN ACCUMULATION ; FLOWER COLORATION ; COLORFUL MODEL ; E3 LIGASE ; DEGRADATION ; PATHWAY ; GENE ; TOLERANCE ; REGULATOR |
WOS Research Area | Plant Sciences |
WOS ID | WOS:000493107700015 |
Publisher | OXFORD UNIV PRESS |
Subtype | Article |
Publication Place | OXFORD |
EISSN | 1460-2431 |
Funding Organization | National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31471909, 31772350] |
Corresponding Author Email | shuqy@ibcas.ac.cn ; wanglsh@ibcas.ac.cn |
OA | Green Published, hybrid |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.ibcas.ac.cn/handle/2S10CLM1/19617 |
Collection | 中科院北方资源植物重点实验室 |
Affiliation | 1.Chinese Acad Sci, Key Lab Plant Resources, Beijing Bot Garden, Inst Bot, Beijing 100093, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Qingdao Agr Univ, Coll Landscape Architecture & Forestry, Qingdao 266109, Shandong, Peoples R China 4.Henan Acad Agr Sci, Inst Hort, Zhengzhou 450002, Henan, Peoples R China |
Recommended Citation 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. |
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