7Y7C

Structure of the Bacterial Ribosome with human tRNA Asp(G34) and mRNA(GAU)

これはPDB形式変換不可エントリーです。

7Y7C の概要

• エントリーDOI: 10.2210/pdb7y7c/pdb
• EMDBエントリー: 33660
• 分子名称: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (56 entities in total)
• 機能のキーワード: trna modifications, decoding, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 2207859.11

構造登録者

Ishiguro, K.,Yokoyama, T.,Shirouzu, M.,Suzuki, T. (登録日: 2022-06-22, 公開日: 2023-10-25, 最終更新日: 2025-02-12)

主引用文献

Zhao, X.,Ma, D.,Ishiguro, K.,Saito, H.,Akichika, S.,Matsuzawa, I.,Mito, M.,Irie, T.,Ishibashi, K.,Wakabayashi, K.,Sakaguchi, Y.,Yokoyama, T.,Mishima, Y.,Shirouzu, M.,Iwasaki, S.,Suzuki, T.,Suzuki, T.
Glycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth.
Cell, 186:5517-, 2023

PubMed Abstract: Transfer RNA (tRNA) modifications are critical for protein synthesis. Queuosine (Q), a 7-deaza-guanosine derivative, is present in tRNA anticodons. In vertebrate tRNAs for Tyr and Asp, Q is further glycosylated with galactose and mannose to generate galQ and manQ, respectively. However, biogenesis and physiological relevance of Q-glycosylation remain poorly understood. Here, we biochemically identified two RNA glycosylases, QTGAL and QTMAN, and successfully reconstituted Q-glycosylation of tRNAs using nucleotide diphosphate sugars. Ribosome profiling of knockout cells revealed that Q-glycosylation slowed down elongation at cognate codons, UAC and GAC (GAU), respectively. We also found that galactosylation of Q suppresses stop codon readthrough. Moreover, protein aggregates increased in cells lacking Q-glycosylation, indicating that Q-glycosylation contributes to proteostasis. Cryo-EM of human ribosome-tRNA complex revealed the molecular basis of codon recognition regulated by Q-glycosylations. Furthermore, zebrafish qtgal and qtman knockout lines displayed shortened body length, implying that Q-glycosylation is required for post-embryonic growth in vertebrates.

PubMed: 37992713
DOI: 10.1016/j.cell.2023.10.026

実験手法

ELECTRON MICROSCOPY (2.51 Å)