MUD1, a RING-v E3 ubiquitin ligase, has an important role in the regulation of pectin methylesterification in Arabidopsis seed coat mucilage

文献类型： 外文期刊

第一作者： Sun, Jinhao

作者： Sun, Jinhao;Yuan, Cuiling;Ding, Anming;Sun, Yuhe;Kong, Yingzhen;Sun, Jinhao;Yuan, Cuiling;Sun, Jinhao;Yuan, Cuiling;Wang, Meng;Chai, Guohua;Zhou, Gongke;Kong, Yingzhen;Zhou, Gongke;Yang, Dahai

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关键词： E3 ubiquitin ligase; MUD1; Pectin methylesterification; RING-V domain

期刊名称：PLANT PHYSIOLOGY AND BIOCHEMISTRY （ 影响因子：4.27； 五年影响因子：4.816 ）

ISSN： 0981-9428

年卷期： 2021 年 168 卷

页码：

收录情况： SCI

摘要： Pectin is one of the major components of plant primary cell wall polysaccharides. The degree of pectin methylesterification (DM) plays an important role in the process of plant growth. However, little is known about the underlying regulatory mechanisms during the process of pectin demethylesterification. Here, we characterized mucilage defect 1 (mud1), a novel Arabidopsis thaliana mutant, which displays increased mucilage adherence resulting from increased activities of pectin methylesterases (PMEs) and decreased degree of pectin methylesterification (DM). MUD1 encodes a nuclear protein with a Really Interesting New Gene (RING)-v domain and is highly expressed in developing seed coat when seed coat mucilage starts to accumulate. We have demonstrated that MUD1 has E3 ubiquitin ligase activity in vitro. The expression of PME-related genes, including MYB52, LUH, SBT1.7, PMEI6, and PMEI14 decreased considerably in mud1. We propose that MUD1 acts as an ubiquitin ligase potentially regulating the DM of pectin by post-transcriptionally removing proteins that normally negatively regulate the level or activity of PMEs in the seed coat mucilage.

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