通过广泛的OB折叠识别tRNA的结构基础
Aline Umuhire Juru1, Rodolfo Ghirlando1, Jinwei Zhang2
1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD, USA.
Nature communications
|July 29, 2024
概括
寡核酸/寡糖酸结合 (OB) 折叠蛋白Trbp通过结合它们的3'端,特别是保存的CA二核酸,来识别转移RNA (tRNA). 这揭示了蛋白质如何与必不可少的RNA分子相互作用的新机制.
科学领域:
- 结构生物学是结构生物学.
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 寡核酸/寡糖结合 (OB) 折叠是一种多功能蛋白质域,参与各种细胞过程,包括核酸和蛋白质识别.
- 细菌Trbp和酵母Arc1p等OB折叠蛋白与转移RNA (tRNA) 代谢有关,但它们的精确结合机制尚不清楚.
研究的目的:
- 阐明由来自Aquifex aeolicus的OB折蛋白Trbp识别tRNA的结构基础.
- 为了研究Trbp和tRNA在3'端之间的分子相互作用.
主要方法:
- 进行X射线晶体学以确定Trbp111与tRNAIle结合的共同晶体结构,分辨率为2.6 Å.
- 针对位点的突变发生和生物物理测试,以验证已识别的相互作用.
主要成果:
- 共同晶体结构显示,Trbp仅通过其3'末端识别tRNA,特别是单链3'CA二核酸.
- OB-fold精确地与终端CA序列及其单链形状相互作用,这是成熟tRNA的普遍特征.
- 酵母Arc1p利用了超越3'端的tRNA体的额外相互作用.
结论:
- 这项研究揭示了由OB折叠介导的tRNA识别的以前未知的模式,重点是3'终端CA二核酸.
- 这些发现为有关tRNA氨基化,折叠,定位,贩运和潜在盗版的蛋白质-tRNA相互作用提供了新的见解.
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