Nucleotide-induced hyper-oligomerization inactivates transcription termination factor ρ

Bing Wang, Nelly Said, Tarek Hilal, Mark Finazzo, Markus C. Wahl () and Irina Artsimovitch ()
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Bing Wang: The Ohio State University
Nelly Said: Takustr. 6
Tarek Hilal: Takustr. 6
Mark Finazzo: The Ohio State University
Markus C. Wahl: Takustr. 6
Irina Artsimovitch: The Ohio State University

Nature Communications, 2025, vol. 16, issue 1, 1-16

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-56824-8

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