6N67

Crystal structure of the ligase domain of fungal tRNA ligase Trl1

6N67 の概要

• エントリーDOI: 10.2210/pdb6n67/pdb
• 分子名称: tRNA ligase, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: rna ligase, trna splicing, inhibitor, atp-binding, ligase
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50233.53

構造登録者

Peschek, J.,Walter, P. (登録日: 2018-11-26, 公開日: 2019-07-03, 最終更新日: 2024-10-23)

主引用文献

Peschek, J.,Walter, P.
tRNA ligase structure reveals kinetic competition between non-conventional mRNA splicing and mRNA decay.
Elife, 8:-, 2019

PubMed Abstract: Yeast tRNA ligase (Trl1) is an essential trifunctional enzyme that catalyzes exon-exon ligation during tRNA biogenesis and the non-conventional splicing of mRNA during the unfolded protein response (UPR). The UPR regulates the protein folding capacity of the endoplasmic reticulum (ER). ER stress activates Ire1, an ER-resident kinase/RNase, which excises an intron from mRNA followed by exon-exon ligation by Trl1. The spliced product encodes for a potent transcription factor that drives the UPR. Here we report the crystal structure of Trl1 RNA ligase domain from at 1.9 Å resolution. Structure-based mutational analyses uncovered kinetic competition between RNA ligation and degradation during mRNA splicing. Incompletely processed mRNA is degraded by Xrn1 and the Ski/exosome complex. We establish cleaved mRNA as endogenous substrate for ribosome-associated quality control. We conclude that mRNA decay and surveillance mechanisms collaborate in achieving fidelity of non-conventional mRNA splicing during the UPR.

PubMed: 31237564
DOI: 10.7554/eLife.44199

実験手法

X-RAY DIFFRACTION (1.9 Å)