IB-CAS  > 中科院北方资源植物重点实验室
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; Zhang, Hechen3; Shu, Qingyan; Wang, Liangsheng1
2019
Source PublicationJOURNAL OF EXPERIMENTAL BOTANY
ISSN0022-0957
Volume70Issue:18Pages:4749-4762
AbstractFlavonoids 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.
KeywordChalcone synthase degradation flavonoid biosynthesis Paeonia RING-H2 ubiquitination
Subject AreaPlant Sciences
DOI10.1093/jxb/erz245
Indexed BySCI
Language英语
WOS KeywordFLAVONOID BIOSYNTHESIS ; ANTHOCYANIN ACCUMULATION ; FLOWER COLORATION ; COLORFUL MODEL ; E3 LIGASE ; DEGRADATION ; PATHWAY ; GENE ; TOLERANCE ; REGULATOR
WOS Research AreaPlant Sciences
WOS IDWOS:000493107700015
PublisherOXFORD UNIV PRESS
SubtypeArticle
Publication PlaceOXFORD
EISSN1460-2431
Funding OrganizationNational Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31471909, 31772350]
Corresponding Author Emailshuqy@ibcas.ac.cn ; wanglsh@ibcas.ac.cn
OAGreen Published, hybrid
Citation statistics
Cited Times:12[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ibcas.ac.cn/handle/2S10CLM1/19617
Collection中科院北方资源植物重点实验室
Affiliation1.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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