特定于背景的核糖体的泛素修饰调节了氧化应激下的翻译
Shannon E Dougherty1, Géssica C Barros1, Matthew W Foster2
1Department of Biology, Duke University, Durham, NC 27708, USA.
bioRxiv : the preprint server for biology
|February 20, 2025
概括
细胞压力会触发特定的核糖体无处不在模式,调节翻译. 研究人员开发了一种新的蛋白质组学方法来绘制这些特定位点的泛素修饰,揭示了动态的压力诱导的变化和新的调节途径.
科学领域:
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
- 蛋白质组学是指蛋白质组学.
背景情况:
- 细胞压力通过核糖体无化激活了转化控制通路.
- 在不同的翻译调节模式中,特定位点的核糖体普遍存在的确切作用尚未完全理解.
研究的目的:
- 开发一种敏感的蛋白质组学方法来量化在核糖体上的特定位点的泛素修饰.
- 在应对细胞压力时,系统地研究核糖体无处不在的模式.
主要方法:
- 开发了一种向蛋白质组学方法,以量化78个核糖体和链接的特定位点泛化.
- 应用该方法来测量对过氧化应激反应中的核糖体泛化.
- 研究了E3结合酶Hel2和E2结合酶Rad6在压力诱导的无化中的作用.
主要成果:
- 即使在稳定状态条件下,也检测到了特定位点的核糖体泛化,在暴露过氧化时,具有动态的,非静态度的增加 (> 4 个数量级).
- 鉴定了与Hel2.2独立的核糖体蛋白 uS10/Rps20 和 uS3/Rps3 的意想不到的无处不在.
- 由压力因素和涉及的酶影响的经过压力特异性无处不在模式的证明.
- 观察到HEL2和RAD6删除对应激反应和翻译的明显影响.
结论:
- 核糖体ubiquitination构成一个动态和选择性的ubiquitin代码,对细胞应激反应至关重要.
- 这些发现揭示了关于细胞应激期间质量控制途径的整合的新见解.
- 网站特定的无处不在模式提供了一个复杂的翻译调节层,以应对各种细胞压力.
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