8Q3P

Bacterial transcription termination factor Rho G150D mutant

8Q3P の概要

• エントリーDOI: 10.2210/pdb8q3p/pdb
• EMDBエントリー: 18132
• 分子名称: Transcription termination factor Rho, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: rho, termination, transcription
• 由来する生物種: Escherichia
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 883229.67

構造登録者

Said, N.,Hilal, T.,Wahl, M.C. (登録日: 2023-08-04, 公開日: 2023-09-27, 最終更新日: 2024-05-22)

主引用文献

Wang, B.,Said, N.,Hilal, T.,Finazzo, M.,Wahl, M.C.,Artsimovitch, I.
Transcription termination factor rho polymerizes under stress.
Biorxiv, 2023

PubMed Abstract: Bacterial RNA helicase ρ is a genome sentinel that terminates synthesis of damaged and junk RNAs that are not translated by the ribosome. Co-transcriptional RNA surveillance by ρ is essential for quality control of the transcriptome during optimal growth. However, it is unclear how bacteria protect their RNAs from overzealous ρ during dormancy or stress, conditions common in natural habitats. Here we used cryogenic electron microscopy, biochemical, and genetic approaches to show that residue substitutions, ADP, or ppGpp promote hyper-oligomerization of ρ. Our results demonstrate that nucleotides bound at subunit interfaces control ρ switching from active hexamers to inactive higher-order oligomers and extended filaments. Polymers formed upon exposure to antibiotics or ppGpp disassemble when stress is relieved, thereby directly linking termination activity to cellular physiology. Inactivation of ρ through hyper-oligomerization is a regulatory strategy shared by RNA polymerases, ribosomes, and metabolic enzymes across all life.

PubMed: 37645988
DOI: 10.1101/2023.08.18.553922

実験手法

ELECTRON MICROSCOPY (3.5 Å)