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Structure paper

TitleThe Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 550, Year 2025
Publish dateJan 9, 2025
AuthorsDaniela Gjorgjevikj / Naveen Kumar / Bing Wang / Tarek Hilal / Nelly Said / Bernhard Loll / Irina Artsimovitch / Ranjan Sen / Markus C Wahl /
PubMed AbstractMany 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 ...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.
External linksNat Commun / PubMed:39788982 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 4.3 Å
Structure data

17637

8peu

EMDB-17637: Rho-ATPgS-Psu complex I
PDB-8peu: Rho-ATPgS-Psu complex III
Method: EM (single particle) / Resolution: 3.7 Å

17639

8pew

EMDB-17639: Rho-ATPgS-Psu complex II
PDB-8pew: Rho-ATPgS-Psu complex III expanded
Method: EM (single particle) / Resolution: 4.3 Å

17640

8pex

EMDB-17640: Rho P167L-ATPgS-Psu complex I
PDB-8pex: Rho P167L-ATPgS-Psu complex II
Method: EM (single particle) / Resolution: 3.1 Å

17641

8pey

EMDB-17641: Rho P167L-ATPgS-Psu complex II
PDB-8pey: Rho P167L-ATPgS-Psu complex II locked
Method: EM (single particle) / Resolution: 3.0 Å

51235

9gcs

EMDB-51235, PDB-9gcs:
Rho-ATP-Psu complex II
Method: EM (single particle) / Resolution: 3.9 Å

51236

9gct

EMDB-51236, PDB-9gct:
Rho-ATP-Psu complex II expanded
Method: EM (single particle) / Resolution: 3.7 Å

51237

9gcu

EMDB-51237, PDB-9gcu:
Rho-P167L-ATP gamma S
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • enterobacteria phage p4 (virus)
KeywordsGENE REGULATION / Transcription termination / Phage inhibitor / TRANSCRIPTION

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