dc.contributor.author
Gjorgjevikj, Daniela
dc.contributor.author
Kumar, Naveen
dc.contributor.author
Wang, Bing
dc.contributor.author
Hilal, Tarek
dc.contributor.author
Said, Nelly
dc.contributor.author
Loll, Bernhard
dc.contributor.author
Artsimovitch, Irina
dc.contributor.author
Sen, Ranjan
dc.contributor.author
Wahl, Markus C.
dc.date.accessioned
2025-02-04T07:11:45Z
dc.date.available
2025-02-04T07:11:45Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/46463
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-46176
dc.description.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.
en
dc.format.extent
20 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
Bacteriophages
en
dc.subject
Cryoelectron microscopy
en
dc.subject
Enzyme mechanisms
en
dc.subject
Transcription factors
en
dc.subject
Transcriptional regulatory elements
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie
dc.title
The Psu protein of phage satellite P4 inhibits transcription termination factor ρ by forced hyper-oligomerization
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
550
dcterms.bibliographicCitation.doi
10.1038/s41467-025-55897-9
dcterms.bibliographicCitation.journaltitle
Nature Communications
dcterms.bibliographicCitation.volume
16
dcterms.bibliographicCitation.url
https://doi.org/10.1038/s41467-025-55897-9
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie

refubium.funding
Springer Nature DEAL
refubium.note.author
Die Publikation wurde aus Open Access Publikationsgeldern der Freien Universität Berlin gefördert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
2041-1723