Widespread gene regulator Psu inhibits transcription termination factor ρ by forced hyper-oligomerization

Author:

Gjorgjevikj Daniela,Kumar Naveen,Wang Bing,Hilal Tarek,Said Nelly,Loll Bernhard,Artsimovitch Irina,Sen Ranjan,Wahl Markus C.ORCID

Abstract

AbstractMany bacteriophages modulate the host transcription machinery for efficient expression of their own genomes. Phage P4 polarity suppression protein, Psu, is a building block of the viral capsid and inhibits the hexameric transcription termination factor, ρ, by presently unknown mechanisms. We elucidated cryogenic electron microscopy structures of ρ-Psu complexes, showing that Psu dimers laterally clamp two inactive, open ρ rings and promote their expansion to higher-oligomeric states. Systematic 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. Bioinformatic analyses suggested that, in addition to guarding its own genome against ρ, Psu enables expression of diverse phage-defense systems commonly found in P4-like mobile genetic elements across bacteria. Thus, Psu is a widespread gene regulator that inhibits ρviaforced hyper-oligomerization.

Publisher

Cold Spring Harbor Laboratory

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