| 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)
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