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| Title | Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ. |
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| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 1653, Year 2025 |
| Publish date | Feb 15, 2025 |
 Authors | Bing Wang / Nelly Said / Tarek Hilal / Mark Finazzo / Markus C Wahl / Irina Artsimovitch /   |
| 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 ...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. |
 External links | Nat Commun / PubMed:39952913 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.4 Å |
| Structure data | EMDB-50352, PDB-9ff7: |
| Chemicals |  ChemComp-ME7:  ChemComp-MG: |
| Source |
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 Keywords | TRANSCRIPTION / Rho / termination / bacterial stress response / ppGpp |
escherichia coli (E. coli)