9FF7

Structure of the BMOE-crosslinked transcription termination factor Rho in the presence of ppGpp; S84C/M405C double mutant

9FF7 の概要

• エントリーDOI: 10.2210/pdb9ff7/pdb
• 関連するPDBエントリー: 8Q3P
• EMDBエントリー: 50352
• 分子名称: Transcription termination factor Rho, 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione), MAGNESIUM ION (3 entities in total)
• 機能のキーワード: rho, transcription, termination, bacterial stress response, ppgpp
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 564851.31

構造登録者

Said, N.,Hilal, T.,Wahl, M.C. (登録日: 2024-05-22, 公開日: 2025-04-09)

主引用文献

Wang, B.,Said, N.,Hilal, T.,Finazzo, M.,Wahl, M.C.,Artsimovitch, I.
Nucleotide-induced hyper-oligomerization inactivates transcription termination factor rho.
Nat Commun, 16:1653-1653, 2025

PubMed Abstract: Bacterial RNA helicase ρ is a genome sentinel that terminates the synthesis of damaged and junk RNAs that are not translated by the ribosome. It is unclear how ρ is regulated during dormancy or stress, when translation is inefficient and RNAs are vulnerable to ρ-mediated release. We use cryogenic electron microscopy, biochemical, and genetic approaches to show that substitutions of residues in the connector between two ρ domains or ADP promote the formation of extended Escherichia coli ρ filaments. By contrast, (p)ppGpp induces the formation of transient ρ dodecamers. Our results demonstrate that ADP and (p)ppGpp nucleotides bound at subunit interfaces inhibit ρ ring closure that underpins the hexamer activation, thus favoring the assembly of inactive higher-order oligomers. Connector substitutions and antibiotics that inhibit RNA and protein syntheses trigger ρ aggregation in the cell. These and other recent data implicate aggregation as a widespread strategy to tune ρ activity.

PubMed: 39952913
DOI: 10.1038/s41467-025-56824-8

実験手法

ELECTRON MICROSCOPY (3.4 Å)