6XE0

Cryo-EM structure of NusG-CTD bound to 70S ribosome (30S: NusG-CTD fragment)

6XE0 の概要

• エントリーDOI: 10.2210/pdb6xe0/pdb
• EMDBエントリー: 22143
• 分子名称: 30S ribosomal protein S2, 30S ribosomal protein S11, 30S ribosomal protein S12, ... (22 entities in total)
• 機能のキーワード: ribosome, nusg, translation
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 784057.86

構造登録者

Washburn, R.,Zuber, P.,Sun, M.,Hashem, Y.,Shen, B.,Li, W.,Harvey, S.,Acosta-Reyes, F.J.,Knauer, S.H.,Frank, J.,Gottesman, M.E. (登録日: 2020-06-11, 公開日: 2020-07-29, 最終更新日: 2024-03-06)

主引用文献

Washburn, R.S.,Zuber, P.K.,Sun, M.,Hashem, Y.,Shen, B.,Li, W.,Harvey, S.,Acosta Reyes, F.J.,Gottesman, M.E.,Knauer, S.H.,Frank, J.
Escherichia coli NusG Links the Lead Ribosome with the Transcription Elongation Complex.
Iscience, 23:101352-101352, 2020

PubMed Abstract: It has been known for more than 50 years that transcription and translation are physically coupled in bacteria, but whether or not this coupling may be mediated by the two-domain protein N-utilization substance (Nus) G in Escherichia coli is still heavily debated. Here, we combine integrative structural biology and functional analyses to provide conclusive evidence that NusG can physically link transcription with translation by contacting both RNA polymerase and the ribosome. We present a cryo-electron microscopy structure of a NusG:70S ribosome complex and nuclear magnetic resonance spectroscopy data revealing simultaneous binding of NusG to RNAP and the intact 70S ribosome, providing the first direct structural evidence for NusG-mediated coupling. Furthermore, in vivo reporter assays show that recruitment of NusG occurs late in transcription and strongly depends on translation. Thus, our data suggest that coupling occurs initially via direct RNAP:ribosome contacts and is then mediated by NusG.

PubMed: 32726726
DOI: 10.1016/j.isci.2020.101352

実験手法

ELECTRON MICROSCOPY (6.8 Å)