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Structural basis for tRNA-dependent cysteine biosynthesis

Author

Listed:
  • Meirong Chen

    (Hokkaido University)

  • Koji Kato

    (Hokkaido University
    Hokkaido University)

  • Yume Kubo

    (Hokkaido University)

  • Yoshikazu Tanaka

    (Hokkaido University
    Hokkaido University
    Japan Science and Technology Agency, PRESTO)

  • Yuchen Liu

    (Louisiana State University)

  • Feng Long

    (University of Georgia)

  • William B. Whitman

    (University of Georgia)

  • Pascal Lill

    (Max Planck Institute of Molecular Physiology)

  • Christos Gatsogiannis

    (Max Planck Institute of Molecular Physiology)

  • Stefan Raunser

    (Max Planck Institute of Molecular Physiology)

  • Nobutaka Shimizu

    (High Energy Accelerator Research Organization (KEK))

  • Akira Shinoda

    (Hokkaido University)

  • Akiyoshi Nakamura

    (National Institute of Advanced Industrial Science and Technology (AIST))

  • Isao Tanaka

    (Hokkaido University)

  • Min Yao

    (Hokkaido University
    Hokkaido University)

Abstract

Cysteine can be synthesized by tRNA-dependent mechanism using a two-step indirect pathway, where O-phosphoseryl-tRNA synthetase (SepRS) catalyzes the ligation of a mismatching O-phosphoserine (Sep) to tRNACys followed by the conversion of tRNA-bounded Sep into cysteine by Sep-tRNA:Cys-tRNA synthase (SepCysS). In ancestral methanogens, a third protein SepCysE forms a bridge between the two enzymes to create a ternary complex named the transsulfursome. By combination of X-ray crystallography, SAXS and EM, together with biochemical evidences, here we show that the three domains of SepCysE each bind SepRS, SepCysS, and tRNACys, respectively, which mediates the dynamic architecture of the transsulfursome and thus enables a global long-range channeling of tRNACys between SepRS and SepCysS distant active sites. This channeling mechanism could facilitate the consecutive reactions of the two-step indirect pathway of Cys-tRNACys synthesis (tRNA-dependent cysteine biosynthesis) to prevent challenge of translational fidelity, and may reflect the mechanism that cysteine was originally added into genetic code.

Suggested Citation

  • Meirong Chen & Koji Kato & Yume Kubo & Yoshikazu Tanaka & Yuchen Liu & Feng Long & William B. Whitman & Pascal Lill & Christos Gatsogiannis & Stefan Raunser & Nobutaka Shimizu & Akira Shinoda & Akiyos, 2017. "Structural basis for tRNA-dependent cysteine biosynthesis," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01543-y
    DOI: 10.1038/s41467-017-01543-y
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