ArticleJournal of molecular biology2015
Architecture of the Complex Formed by Large and Small Terminase Subunits from Bacteriophage P22.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Variable Assembly and Procapsid Binding of Bacteriophage P22 Terminase Subunits in Solution.Pathogens (Basel, Switzerland) · 2024Article
- Article
- Biophysical and structural characterization of a multifunctional viral genome packaging motor.Nucleic acids research · 2024Article
- Molecular Architecture of Salmonella Typhimurium Virus P22 Genome Ejection Machinery.Journal of molecular biology · 2023Article
- Complete genome sequences of microbacterium phages Tedro and BAjuniper.Microbiology resource announcements · 2023Article
- Cryo-EM for Small Molecules.Current protocols · 2022Review
- 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
- Isolation and Characterization of the LyticViruses · 2022Article
- Mass Spectrometry-Based Structural Virology.Analytical chemistry · 2021Review
- Biophysical analysis of Pseudomonas-phage PaP3 small terminase suggests a mechanism for sequence-specific DNA-binding by lateral interdigitation.Nucleic acids research · 2020Article
- Recognition of an α-helical hairpin in P22 large terminase by a synthetic antibody fragment.Acta crystallographica. Section D, Structural biology · 2020Article
- Review
- Bacteriophage N4 large terminase: expression, purification and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Cryo-EM Elucidation of the Structure of Bacteriophage P22 Virions after Genome Release.Biophysical journal · 2018Article
- Review
- Physical and Functional Characterization of a Viral Genome Maturation Complex.Biophysical journal · 2017Article
- Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.Nature communications · 2017Article
- Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The Journal of biological chemistry · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Packaging of viral genomes inside empty procapsids is driven by a powerful ATP-hydrolyzing motor, formed in many double-stranded DNA viruses by a complex of a small terminase (S-terminase) subunit and a large terminase (L-terminase) subunit, transiently docked at the portal vertex during genome packaging. Despite recent progress in elucidating the structure of individual terminase subunits and their domains, little is known about the architecture of an assembled terminase complex. Here, we describe a bacterial co-expression system that yields milligram quantities of the S-terminase:L-terminase complex of the Salmonella phage P22. In vivo assembled terminase complex was affinity-purified and stabilized by addition of non-hydrolyzable ATP, which binds specifically to the ATPase domain of L-terminase. Mapping studies revealed that the N-terminus of L-terminase ATPase domain (residues 1-58) contains a minimal S-terminase binding domain sufficient for stoichiometric association with residues 140-162 of S-terminase, the L-terminase binding domain. Hydrodynamic analysis by analytical ultracentrifugation sedimentation velocity and native mass spectrometry revealed that the purified terminase complex consists predominantly of one copy of the nonameric S-terminase bound to two equivalents of L-terminase (1S-terminase:2L-terminase). Direct visualization of this molecular assembly in negative-stained micrographs yielded a three-dimensional asymmetric reconstruction that resembles a "nutcracker" with two L-terminase protomers projecting from the C-termini of an S-terminase ring. This is the first direct visualization of a purified viral terminase complex analyzed in the absence of DNA and procapsid.
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