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

© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 70(2019), 18 vom: 24. Sept., Seite 4749-4762
1. Verfasser: Gu, Zhaoyu (VerfasserIn)
Weitere Verfasser: Men, Siqi, Zhu, Jin, Hao, Qing, Tong, Ningning, Liu, Zheng-An, Zhang, Hechen, Shu, Qingyan, Wang, Liangsheng
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Paeonia Chalcone synthase RING-H2 degradation flavonoid biosynthesis ubiquitination Plant Proteins Acyltransferases mehr... EC 2.3.- flavanone synthetase EC 2.3.1.74 Ubiquitin-Protein Ligases EC 2.3.2.27
Beschreibung
Zusammenfassung:© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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
Beschreibung:Date Completed 27.07.2020
Date Revised 27.07.2020
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erz245