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Structural insight into precursor tRNA processing by yeast ribonuclease P

作者:Pengfei Lan, Ming Tan, Yuebin Zhang, Shuangshuang Niu, Juan Chen, Shaohua Shi, Shuwan Qiu, Xuejuan Wang, Xiangda Peng, Gang Cai, Hong Cheng, Jian Wu, Guohui Li, Ming Lei · 发表于:Science · 年份:2018 · DOI:10.1126/science.aat6678 · 被引用次数:90 · 研究领域:RNA modifications and cancer、RNA and protein synthesis mechanisms、RNA Research and Splicing

Structures of eukaryotic ribonuclease P Ribonuclease P (RNase P) is a ribozyme that processes transfer RNA (tRNA) precursors and is found in all three kingdoms of life. Now, Lan et al. report the structures of yeast RNase P (see the Perspective by Scott and Nagai). The aporibozyme structure reveals how the protein components stabilize the RNA and explains how the structural roles of bacterial RNA elements have been delegated to the protein components in RNase P of higher organisms during evolution. The structure of yeast RNase P in complex with its natural substrate, a tRNA precursor, demonstrates the structural basis for substrate recognition and provides insights into its catalytic mechanism. Science , this issue p. eaat6678 ; see also p. 644