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Structural basis for tRNA-dependent cysteine biosynthesis

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/67911

Title: Structural basis for tRNA-dependent cysteine biosynthesis
Authors: Chen, Meirong Browse this author
Kato, Koji Browse this author
Kubo, Yume Browse this author
Tanaka, Yoshikazu Browse this author
Liu, Yuchen Browse this author
Long, Feng Browse this author
Whitman, William B. Browse this author
Lill, Pascal Browse this author
Gatsogiannis, Christos Browse this author
Raunser, Stefan Browse this author
Shimizu, Nobutaka Browse this author
Shinoda, Akira Browse this author
Nakamura, Akiyoshi Browse this author
Tanaka, Isao Browse this author
Yao, Min Browse this author →KAKEN DB
Keywords: Electron microscopy
SAXS
tRNAs
X-ray crystallography
Issue Date: 15-Nov-2017
Publisher: Nature Publishing Group
Journal Title: Nature communications
Volume: 8
Start Page: 1521
Publisher DOI: 10.1038/s41467-017-01543-y
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 tRNA(Cys) 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 tRNA(Cys), respectively, which mediates the dynamic architecture of the transsulfursome and thus enables a global long-range channeling of tRNA(Cys) between SepRS and SepCysS distant active sites. This channeling mechanism could facilitate the consecutive reactions of the two-step indirect pathway of Cys-tRNA(Cys) synthesis (tRNA-dependent cysteine biosynthesis) to prevent challenge of translational fidelity, and may reflect the mechanism that cysteine was originally added into genetic code.
Rights: http://creativecommons.org/licenses/by/4.0/
Type: article
URI: http://hdl.handle.net/2115/67911
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 姚 閔

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