EMD-51235
Rho-ATP-Psu complex II
EMD-51235
Single-particle3.9 Å
![EMD-51235](https://www.ebi.ac.uk/emdb/images/entry/EMD-51235/400_51235.gif)
Map released: 09/10/2024
Last modified: 22/01/2025
Sample Organism:
Escherichia coli,
Enterobacteria phage P4
Sample: Complex of E. coli transcription termination factor Rho with ATP and P4 polarity suppression protein Psu
Fitted models: 9gcs (Avg. Q-score: 0.276)
Deposition Authors: Gjorgjevikj D
,
Wahl MC
,
Hilal T
,
Loll B
Sample: Complex of E. coli transcription termination factor Rho with ATP and P4 polarity suppression protein Psu
Fitted models: 9gcs (Avg. Q-score: 0.276)
Deposition Authors: Gjorgjevikj D
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The Psu protein of phage satellite P4 inhibits transcription termination factor rho by forced hyper-oligomerization.
Gjorgjevikj D
,
Kumar N
,
Wang B
,
Hilal T
,
Said N
,
Loll B
,
Artsimovitch I
,
Sen R,
Wahl MC
(2025) Nat Commun , 16 , 550 - 550
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![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
![](http://www.ebi.ac.uk/web_guidelines/images/logos/orcid/orcid_16x16.png)
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(2025) Nat Commun , 16 , 550 - 550
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.
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.