期刊
PLANT AND CELL PHYSIOLOGY
卷 58, 期 11, 页码 1953-1962出版社
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcx129
关键词
Anthocyanin; posttranslational modification; transcription factor MdMYB1; ubiquitination; ubiquitin E3 ligase MdMIEL1
资金
- NSFC, Ministry of Education of China [31325024, 31471854, 31601742, IRT15R42]
- Ministry of Agriculture of China [CARS-28]
- Shandong Province [SDAIT-06-03]
MdMYB1 is an important regulator for anthocyanin accumulation in apple (Malus x domestica). Here, an apple RING E3 ligase, MdMIEL1, was screened out as a partner of MdMYB1 with a yeast two-hybrid approach. Pull-down, bimolecular fluorescence complementation and coimmunoprecipitation assays further verified the interaction between MdMIEL1 and MdMYB1 proteins. Subsequently, in vitro and in vivo experiments indicated that MdMIEL1 functioned as a ubiquitin E3 ligase to ubiquitinate MdMYB1 protein, followed by degradation through a 26S proteasome pathway. Furthermore, transgenic studies in apple calli and Arabidopsis demonstrated that MdMIEL1 negatively regulated anthocyanin accumulation by modulating the degradation of MdMYB1 protein. Taken together, our findings provide a new insight into the molecular mechanism by which MdMIEL1 negatively regulates anthocyanin biosynthesis by ubiquitinating and degrading MdMYB1 protein.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据