The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization

Daniela Gjorgjevikj, Naveen Kumar, Bing Wang, Tarek Hilal, Nelly Said, Bernhard Loll, Irina Artsimovitch, Ranjan Sen and Markus C. Wahl ()
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Daniela Gjorgjevikj: Freie Universität Berlin
Naveen Kumar: Centre for DNA Fingerprinting and Diagnostics
Bing Wang: The Ohio State University
Tarek Hilal: Freie Universität Berlin
Nelly Said: Freie Universität Berlin
Bernhard Loll: Freie Universität Berlin
Irina Artsimovitch: The Ohio State University
Ranjan Sen: Centre for DNA Fingerprinting and Diagnostics
Markus C. Wahl: Freie Universität Berlin

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: Abstract Many bacteriophages modulate host transcription to favor expression of their own genomes. Phage satellite P4 polarity suppression protein, Psu, a building block of the viral capsid, inhibits hexameric transcription termination factor, ρ, by presently unknown mechanisms. Our cryogenic electron microscopy structures of ρ-Psu complexes show that Psu dimers clamp two inactive, open ρ rings and promote their expansion to higher-oligomeric states. ATPase, nucleotide binding and nucleic acid binding studies revealed that Psu hinders ρ ring closure and traps nucleotides in their binding pockets on ρ. Structure-guided mutagenesis in combination with growth, pull-down, and termination assays further delineated the functional ρ-Psu interfaces in vivo. Bioinformatic analyses revealed that Psu is associated with a wide variety of phage defense systems across Enterobacteriaceae, suggesting that Psu may regulate expression of anti-phage genes. Our findings show that modulation of the ρ oligomeric state via diverse strategies is a pervasive gene regulatory principle in bacteria.

Date: 2025
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DOI: 10.1038/s41467-025-55897-9

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