Enrichment and analysis of rice seedling ubiquitin-related proteins using four UBA domains (GST-qUBAs)

文献类型： 外文期刊

第一作者： Meng, Qingshi

作者： Meng, Qingshi;Rao, Liqun;Meng, Qingshi;Pan, Yinghong;Meng, Qingshi;Pan, Yinghong

作者机构：

关键词： Oryza sativa;Ubiquitin;Ubiquitin-associated domain;Ubiquitin ligases;Affinity enrichment;Mass spectrometry

期刊名称：PLANT SCIENCE （ 影响因子：4.729； 五年影响因子：5.132 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Protein ubiquitination is a common posttranslational modification that often occurs on lysine residues. It controls the half-life, interaction and trafficking of intracellular proteins and is involved in different plant development stages and responses to environment stresses. Four Ubiquitin-Associated (UBA) domains were sequentially fused with Glutathione S-transferase (GST) tag (GST-qUBA) as bait protein in this study. A two-step affinity protocol was successfully developed and the identification of ubiquitinated proteins and their interaction proteins increased almost threefold compared to methods that directly identify ubiquitinated proteins from crude samples. A total of 170 ubiquitin-related proteins were identified in GST-qUBAs enriched samples taken from rice seedlings. There were 134 ubiquitinated proteins, 5 ubiquitin-activating enzymes (E1s), 5 ubiquitin-conjugating enzymes (E2s), 19 ubiquitin ligases (E3s) and 7 deubiquitinating enzymes (DUBs), which all contained various key factors that regulated a wide range of biological processes. Moreover, a series of novel ubiquitinated proteins and E3s were identified that had not been previously reported. This study investigated a high-efficiency method for identifying novel ubiquitinated proteins involved in biological processes and a primary mapping of the ubiquitylome during rice seedling development, which could extend our understanding of how ubiquitin modification regulates plant proteins, pathways and cellular processes. (C) 2014 Elsevier Ireland Ltd. All rights reserved.

分类号： Q94

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