8pex | pdb_00008pex
Rho P167L-ATPgS-Psu complex II
Structural highlights
FunctionRHO_ECOLI Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884] Publication Abstract from PubMedMany 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, rho, by presently unknown mechanisms. Our cryogenic electron microscopy structures of rho-Psu complexes show that Psu dimers clamp two inactive, open rho rings and promote their expansion to higher-oligomeric states. ATPase, nucleotide binding and nucleic acid binding studies revealed that Psu hinders rho ring closure and traps nucleotides in their binding pockets on rho. Structure-guided mutagenesis in combination with growth, pull-down, and termination assays further delineated the functional rho-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 rho oligomeric state via diverse strategies is a pervasive gene regulatory principle in bacteria. 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 Nat Commun. 2025 Jan 9;16(1):550. doi: 10.1038/s41467-025-55897-9. PMID:39788982[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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