9FF7
Structure of the BMOE-crosslinked transcription termination factor Rho in the presence of ppGpp; S84C/M405C double mutant
Summary for 9FF7
Entry DOI | 10.2210/pdb9ff7/pdb |
Related | 8Q3P |
EMDB information | 50352 |
Descriptor | Transcription termination factor Rho, 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione), MAGNESIUM ION (3 entities in total) |
Functional Keywords | rho, transcription, termination, bacterial stress response, ppgpp |
Biological source | Escherichia coli |
Total number of polymer chains | 12 |
Total formula weight | 564851.31 |
Authors | |
Primary citation | 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 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: 39952913DOI: 10.1038/s41467-025-56824-8 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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