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Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase engaged in translational control

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Item Type:Article
Title:Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase engaged in translational control
Creators Name:Yang, J.Y. and Deng, X.Y. and Li, Y.S. and Ma, X.C. and Feng, J.X. and Yu, B. and Chen, Y. and Luo, Y.L. and Wang, X. and Chen, M.L. and Fang, Z.X. and Zheng, F.X. and Li, Y.P. and Zhong, Q. and Kang, T.B. and Song, L.B. and Xu, R.H. and Zeng, M.S. and Chen, W. and Zhang, H. and Xie, W. and Gao, S.
Abstract:Cleavage of transfer (t)RNA and ribosomal (r)RNA are critical and conserved steps of translational control for cells to overcome varied environmental stresses. However, enzymes that are responsible for this event have not been fully identified in high eukaryotes. Here, we report a mammalian tRNA/rRNA-targeting endoribonuclease: SLFN13, a member of the Schlafen family. Structural study reveals a unique pseudo-dimeric U-pillow-shaped architecture of the SLFN13 N'-domain that may clamp base-paired RNAs. SLFN13 is able to digest tRNAs and rRNAs in vitro, and the endonucleolytic cleavage dissevers 11 nucleotides from the 3'-terminus of tRNA at the acceptor stem. The cytoplasmically localised SLFN13 inhibits protein synthesis in 293T cells. Moreover, SLFN13 restricts HIV replication in a nucleolytic activity-dependent manner. According to these observations, we term SLFN13 RNase S13. Our study provides insights into the modulation of translational machinery in high eukaryotes, and sheds light on the functional mechanisms of the Schlafen family.
Keywords:alpha-Helical Protein Conformation, beta-Strand Protein Conformation, Binding Sites, Cytoplasm, Endoribonucleases, Molecular Cloning, Escherichia coli, Gene Expression, Genetic Vectors, HEK293 Cells, HIV-1, Kinetics, Molecular Models, Protein Binding, Protein Biosynthesis, Protein Interaction Domains and Motifs, Recombinant Proteins, Ribosomal RNA, RNA Cleavage, Substrate Specificity, Transfer RNA, Virus Replication, X-Ray Crystallography
Source:Nature Communications
ISSN:2041-1723
Publisher:Nature Publishing Group
Volume:9
Number:1
Page Range:1165
Date:21 March 2018
Official Publication:https://doi.org/10.1038/s41467-018-03544-x
PubMed:View item in PubMed

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