Structural basis for tRNA-dependent cysteine biosynthesis

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, Akiyoshi Nakamura, Isao Tanaka and Min Yao ()
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Meirong Chen: Hokkaido University
Koji Kato: Hokkaido University
Yume Kubo: Hokkaido University
Yoshikazu Tanaka: Hokkaido University
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

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: 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.

Date: 2017
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DOI: 10.1038/s41467-017-01543-y

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