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9FF7

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

Summary for 9FF7
Entry DOI10.2210/pdb9ff7/pdb
Related8Q3P
EMDB information50352
DescriptorTranscription termination factor Rho, 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione), MAGNESIUM ION (3 entities in total)
Functional Keywordsrho, transcription, termination, bacterial stress response, ppgpp
Biological sourceEscherichia coli
Total number of polymer chains12
Total formula weight564851.31
Authors
Said, N.,Hilal, T.,Wahl, M.C. (deposition date: 2024-05-22, release date: 2025-04-09)
Primary citationWang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

242842

數據於2025-10-08公開中

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