Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress
Site-Specific K63 Ubiquitinomics Provides Insights into Translation Regulation under Stress
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DOI：
10.1021/acs.jproteome.8b00623
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发表时间：
2019-01-01
影响因子：
4.4
通讯作者：
Silva, Gustavo M.
中科院分区：
文献类型：
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作者：
Back, Songhee;Gorman, Andrew W.;Silva, Gustavo M.
在氧化应激期间，K63连接的多聚泛素链修饰多种蛋白质，包括核糖体。了解K63泛素的精确位点是了解其在应激反应中功能的关键。为了鉴定K63泛素的位点，我们开发了一种新的基于质谱的方法，该方法定量了酵母中对H2O2诱导的氧化应激反应的> 1100个K63泛素化位点。我们确定，在压力下，K63泛素修饰的蛋白质参与了几种细胞功能，包括离子转运，蛋白质运输和翻译。最丰富的泛素位点定位于核糖体的40S亚基的头部，修饰组装的多聚核糖体，并影响翻译因子的结合。这些结果表明，在氧化应激过程中的翻译后启动控制的新途径，并说明了高分辨率映射的非典型泛素化事件的重要性。
During oxidative stress, K63-linked polyubiquitin chains modify a variety of proteins including ribosomes. Knowledge of the precise sites of K63 ubiquitin is key to understand its function during the response to stress. To identify the sites of K63 ubiquitin, we developed anew mass spectrometry based method that quantified >1100 K63 ubiquitination sites in yeast that responded to oxidative stress induced by H2O2. We determined that under stress, K63 ubiquitin-modified proteins were involved in several cellular functions including ion transport, protein trafficking, and translation. The most abundant ubiquitin sites localized to the head of the 40S subunit of the ribosome, modified assembled polysomes, and affected the binding of translation factors. The results suggested a new pathway of post-initiation control of translation during oxidative stress and illustrated the importance of high-resolution mapping of noncanonical ubiquitination events.