ArticleNucleic acids research2020
Biophysical analysis of Pseudomonas-phage PaP3 small terminase suggests a mechanism for sequence-specific DNA-binding by lateral interdigitation.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Computational prediction resolves thousands of homooligomeric phage protein structures.bioRxiv : the preprint server for biology · 2026Article
- Bacteriophage deploys a RecA-dependent nuclease to inhibit Staphylococcus aureus replication and promote phage propagation.Nucleic acids research · 2026Article
- High-resolution Cryo-EM Analysis of the Therapeutic Pseudomonas Phage Pa223.Journal of molecular biology · 2025Article
- Multidrug-resistantFrontiers in microbiology · 2025Review
- Structural basis for DNA recognition by a viral genome-packaging machine.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Genomic analysis of vB_PaS-HSN4 bacteriophage and its antibacterial activity (in vivo and in vitro) against Pseudomonas aeruginosa isolated from burn.Scientific reports · 2024Article
- Expansion ofViruses · 2023Article
- Reconstruction of 3D density from solution scattering.Methods in enzymology · 2023Article
- Terminase Subunits from the Pseudomonas-Phage E217.Journal of molecular biology · 2022Article
- Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function.Viruses · 2022Review
- Cryo-EM Structure of a Kinetically Trapped Dodecameric Portal Protein from the Pseudomonas-phage PaP3.Journal of molecular biology · 2022Article
- Complete Genome Sequence of Stenotrophomonas maltophilia Siphophage Silvanus.Microbiology resource announcements · 2022Article
- Isolation and characterization of two homolog phages infectingFrontiers in microbiology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The genome packaging motor of tailed bacteriophages and herpesviruses is a powerful nanomachine built by several copies of a large (TerL) and a small (TerS) terminase subunit. The motor assembles transiently at the portal vertex of an empty precursor capsid (or procapsid) to power genome encapsidation. Terminase subunits have been studied in-depth, especially in classical bacteriophages that infect Escherichia coli or Salmonella, yet, less is known about the packaging motor of Pseudomonas-phages that have increasing biomedical relevance. Here, we investigated the small terminase subunit from three Podoviridae phages that infect Pseudomonas aeruginosa. We found TerS is polymorphic in solution but assembles into a nonamer in its high-affinity heparin-binding conformation. The atomic structure of Pseudomonas phage PaP3 TerS, the first complete structure for a TerS from a cos phage, reveals nine helix-turn-helix (HTH) motifs asymmetrically arranged around a β-stranded channel, too narrow to accommodate DNA. PaP3 TerS binds DNA in a sequence-specific manner in vitro. X-ray scattering and molecular modeling suggest TerS adopts an open conformation in solution, characterized by dynamic HTHs that move around an oligomerization core, generating discrete binding crevices for DNA. We propose a model for sequence-specific recognition of packaging initiation sites by lateral interdigitation of DNA.
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