Journal Article

Apple RING E3 ligase MdMIEL1 inhibits anthocyanin accumulation by ubiquitinating and degrading MdMYB1 protein

Jian-Ping An, Xin Liu, Hao-Hao Li, Chun-Xiang You, Xiao-Fei Wang and Yu-Jin Hao

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 58, issue 11, pages 1953-1962
Published in print November 2017 | ISSN: 0032-0781
Published online September 2017 | e-ISSN: 1471-9053 | DOI: https://dx.doi.org/10.1093/pcp/pcx129
Apple RING E3 ligase MdMIEL1 inhibits anthocyanin accumulation by ubiquitinating and degrading MdMYB1 protein

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Abstract

MdMYB1 is an important regulator for anthocyanin accumulation in apple (Malusdomestica). 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.

Keywords: Anthocyanin; posttranslational modification; transcription factor MdMYB1; ubiquitination; ubiquitin E3 ligase MdMIEL1

Journal Article.  6101 words.  Illustrated.

Subjects: Molecular Biology and Genetics ; Biotechnology ; Biochemistry ; Bioinformatics and Computational Biology ; Molecular and Cell Biology ; Plant Sciences and Forestry ; Plant Physiology

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