Structural basis for tRNA-dependent cysteine biosynthesis

Chen, Meirong; Kato, Koji; Kubo, Yume et al.

Nature communications, 2017, 8, 1521

Permalink : https://hdl.handle.net/2115/67911

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論文情報

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アクセス権
open access
URI
https://hdl.handle.net/2115/67911
タイトル
Structural basis for tRNA-dependent cysteine biosynthesis
著者
Chen, Meirong ; Kato, Koji ; Kubo, Yume ; Tanaka, Yoshikazu ; Liu, Yuchen ; Long, Feng ; Whitman, William B. ; Lill, Pascal ; Gatsogiannis, Christos ; Raunser, Stefan ; Shimizu, Nobutaka ; Shinoda, Akira ; Nakamura, Akiyoshi ; Tanaka, Isao ; Yao, Min
著者名
Chen, Meirong
著者名
Kato, Koji
著者名
Kubo, Yume
著者名
Tanaka, Yoshikazu
著者名
Liu, Yuchen
著者名
Long, Feng
著者名
Whitman, William B.
著者名
Lill, Pascal
著者名
Gatsogiannis, Christos
著者名
Raunser, Stefan
著者名
Shimizu, Nobutaka
著者名
Shinoda, Akira
著者名
Nakamura, Akiyoshi
著者名
Tanaka, Isao
e-Rad_Researcher
40311518
著者名
Yao, Min
言語
英語
キーワード
Electron microscopy
SAXS
tRNAs
X-ray crystallography
発行日
2017-11-15
出版者
Nature Publishing Group
収録物名
Nature communications
巻(号)
8
ページ
1521
抄録
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.
資源タイプ
学術雑誌論文
出版タイプ
Version of Record
権利情報
Creative Commons Attribution 4.0 International
PISSN
2041-1723
関連情報 (isIdenticalTo)
出版社版DOI
https://doi.org/10.1038/s41467-017-01543-y