Structural insight into precursor tRNA processing by yeast ribonuclease P
Science 362(6514):657 eaat6678 Nov 2018 

Lan, Pengfei; Tan, Ming; Zhang, Yuebin; Niu, Shuangshuang; Chen, Juan; Shi, Shaohua; Qiu, Shuwan; Wang, Xuejuan; Peng, Xiangda; Cai, Gang; Cheng, Hong; Wu, Jian; Li, Guohui; Lei, Ming


Ribonuclease P (RNase P) is a universal ribozyme responsible for processing the 5'-leader of pre-transfer RNA (pre-tRNA). Here, we report the 3.5-angstrom cryo-electron microscopy structures ofSaccharomyces cerevisiaeRNase P alone and in complex with pre-tRNAPheThe protein components form a hook-shaped architecture that wraps around the RNA and stabilizes RNase P into a measuring device with two fixed anchors that recognize the L-shaped pre-tRNA. A universally conserved uridine nucleobase and phosphate backbone in the catalytic center together with the scissile phosphate and the O3' leaving group of pre-tRNA jointly coordinate two catalytic magnesium ions. Binding of pre-tRNA induces a conformational change in the catalytic center that is required for catalysis. Moreover, simulation analysis suggests a two-metal-ion SN2 reaction pathway of pre-tRNA cleavage. These results not only reveal the architecture of yeast RNase P but also provide a molecular basis of how the 5'-leader of pre-tRNA is processed by eukaryotic RNase P. 

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