Structural insight into precursor tRNA processing by yeast ribonuclease P

Author:

Lan Pengfei1ORCID,Tan Ming23ORCID,Zhang Yuebin4ORCID,Niu Shuangshuang235ORCID,Chen Juan1,Shi Shaohua1,Qiu Shuwan6,Wang Xuejuan6ORCID,Peng Xiangda4ORCID,Cai Gang6ORCID,Cheng Hong2,Wu Jian1ORCID,Li Guohui4ORCID,Lei Ming1789ORCID

Affiliation:

1. Shanghai Institute of Precision Medicine, Ninth People’s Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200125, China.

2. State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences (CAS), Shanghai 200031, China.

3. University of Chinese Academy of Sciences, CAS, Shanghai 200031, China.

4. Laboratory of Molecular Modeling and Design, State Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, CAS, Dalian 116023, China.

5. School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.

6. Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China.

7. Key laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.

8. National Facility for Protein Science in Shanghai, Zhangjiang Laboratory, Shanghai, 201210, China.

9. Shanghai Science Research Center, CAS, Shanghai, 201204, China.

Abstract

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

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference101 articles.

1. S. Altman L. A. Kirsebom in Ribonuclease P: In The RNA World R. Gesteland T. Cech J. Atkins Eds. (Cold Spring Harbor Laboratory Press ed. 2 1999) chap. 14 pp. 351–378.

2. Of proteins and RNA: The RNase P/MRP family

3. RNase P: interface of the RNA and protein worlds

4. Ribonuclease P: The Evolution of an Ancient RNA Enzyme

5. Higher order folding and domain analysis of the ribozyme from Bacillus subtilis ribonuclease P

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