Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase engaged in translational control
Jin-Yu Yang,
Xiang-Yu Deng,
Yi-Sheng Li,
Xian-Cai Ma,
Jian-Xiong Feng,
Bing Yu,
Yang Chen,
Yi-Ling Luo,
Xi Wang,
Mei-Ling Chen,
Zhi-Xin Fang,
Fu-Xiang Zheng,
Yi-Ping Li,
Qian Zhong,
Tie-Bang Kang,
Li-Bing Song,
Rui-Hua Xu,
Mu-Sheng Zeng,
Wei Chen,
Hui Zhang,
Wei Xie () and
Song Gao ()
Additional contact information
Jin-Yu Yang: Sun Yat-Sen University Cancer Center
Xiang-Yu Deng: Sun Yat-Sen University
Yi-Sheng Li: Berlin Institute for Medical Systems Biology
Xian-Cai Ma: Sun Yat-Sen University
Jian-Xiong Feng: Sun Yat-Sen University Cancer Center
Bing Yu: Sun Yat-Sen University Cancer Center
Yang Chen: Sun Yat-Sen University Cancer Center
Yi-Ling Luo: Sun Yat-Sen University Cancer Center
Xi Wang: Berlin Institute for Medical Systems Biology
Mei-Ling Chen: Sun Yat-Sen University Cancer Center
Zhi-Xin Fang: Sun Yat-Sen University Cancer Center
Fu-Xiang Zheng: Sun Yat-Sen University
Yi-Ping Li: Sun Yat-Sen University
Qian Zhong: Sun Yat-Sen University Cancer Center
Tie-Bang Kang: Sun Yat-Sen University Cancer Center
Li-Bing Song: Sun Yat-Sen University Cancer Center
Rui-Hua Xu: Sun Yat-Sen University Cancer Center
Mu-Sheng Zeng: Sun Yat-Sen University Cancer Center
Wei Chen: Southern University of Science and Technology
Hui Zhang: Sun Yat-Sen University
Wei Xie: Sun Yat-Sen University
Song Gao: Sun Yat-Sen University Cancer Center
Nature Communications, 2018, vol. 9, issue 1, 1-13
Abstract:
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.
Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (3)
Downloads: (external link)
https://www.nature.com/articles/s41467-018-03544-x Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03544-x
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-018-03544-x
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().