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

Author

Listed:
  • 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
    Southern University of Science and Technology)

  • 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
    National Institute of Health)

  • Yi-Ling Luo

    (Sun Yat-Sen University Cancer Center)

  • Xi Wang

    (Berlin Institute for Medical Systems Biology
    German Cancer Research Center)

  • 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
    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)

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.

Suggested Citation

  • 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-, 2018. "Structure of Schlafen13 reveals a new class of tRNA/rRNA- targeting RNase engaged in translational control," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03544-x
    DOI: 10.1038/s41467-018-03544-x
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    Cited by:

    1. Felix J. Metzner & Simon J. Wenzl & Michael Kugler & Stefan Krebs & Karl-Peter Hopfner & Katja Lammens, 2022. "Mechanistic understanding of human SLFN11," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. Jie Chen & Nan Liu & Yinpin Huang & Yuanxun Wang & Yuxing Sun & Qingcui Wu & Dianrong Li & Shuanhu Gao & Hong-Wei Wang & Niu Huang & Xiangbing Qi & Xiaodong Wang, 2021. "Structure of PDE3A–SLFN12 complex and structure-based design for a potent apoptosis inducer of tumor cells," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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