5XLN

Crystal structure of the TRS_UNE-T and 4EHP complex

5XLN の概要

• エントリーDOI: 10.2210/pdb5xln/pdb
• 分子名称: Eukaryotic translation initiation factor 4E type 2, Threonine--tRNA ligase, cytoplasmic (3 entities in total)
• 機能のキーワード: trs, 4ehp, complex, rna binding protein-ligase complex, rna binding protein/ligase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27050.80

構造登録者

Hwang, J.,Nguyen, L.T.,Kim, M.H. (登録日: 2017-05-11, 公開日: 2018-11-21, 最終更新日: 2024-03-27)

主引用文献

Jeong, S.J.,Park, S.,Nguyen, L.T.,Hwang, J.,Lee, E.Y.,Giong, H.K.,Lee, J.S.,Yoon, I.,Lee, J.H.,Kim, J.H.,Kim, H.K.,Kim, D.,Yang, W.S.,Kim, S.Y.,Lee, C.Y.,Yu, K.,Sonenberg, N.,Kim, M.H.,Kim, S.
A threonyl-tRNA synthetase-mediated translation initiation machinery.
Nat Commun, 10:1357-1357, 2019

PubMed Abstract: A fundamental question in biology is how vertebrates evolved and differ from invertebrates, and little is known about differences in the regulation of translation in the two systems. Herein, we identify a threonyl-tRNA synthetase (TRS)-mediated translation initiation machinery that specifically interacts with eIF4E homologous protein, and forms machinery that is structurally analogous to the eIF4F-mediated translation initiation machinery via the recruitment of other translation initiation components. Biochemical and RNA immunoprecipitation analyses coupled to sequencing suggest that this machinery emerged as a gain-of-function event in the vertebrate lineage, and it positively regulates the translation of mRNAs required for vertebrate development. Collectively, our findings demonstrate that TRS evolved to regulate vertebrate translation initiation via its dual role as a scaffold for the assembly of initiation components and as a selector of target mRNAs. This work highlights the functional significance of aminoacyl-tRNA synthetases in the emergence and control of higher order organisms.

PubMed: 30902983
DOI: 10.1038/s41467-019-09086-0

実験手法

X-RAY DIFFRACTION (1.9 Å)