ArticleJournal of virology2012
Portal-large terminase interactions of the bacteriophage T4 DNA packaging machine implicate a molecular lever mechanism for coupling ATPase to DNA translocation.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Metagenomic selections reveal diverse antiphage defenses in human and environmental microbiomes.Cell host & microbe · 2025Article
- Comparative Genomic Analysis of 66 Bacteriophages Infecting Morganella morganii Strains.Current microbiology · 2025Article
- Variable Assembly and Procapsid Binding of Bacteriophage P22 Terminase Subunits in Solution.Pathogens (Basel, Switzerland) · 2024Article
- Review
- The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain.Nucleic acids research · 2017Article
- Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.Nature communications · 2017Article
- Mechanisms of DNA Packaging by Large Double-Stranded DNA Viruses.Annual review of virology · 2015Review
- Structure and mechanism of the ATPase that powers viral genome packaging.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution.Nature communications · 2015Article
- Molecular interactions and residues involved in force generation in the T4 viral DNA packaging motor.Journal of molecular biology · 2014Article
- Single-molecule packaging initiation in real time by a viral DNA packaging machine from bacteriophage T4.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- T4 bacteriophage as a phage display platform.Archives of microbiology · 2014Review
- Evidence for an electrostatic mechanism of force generation by the bacteriophage T4 DNA packaging motor.Nature communications · 2014Article
- Structure-function analysis of the DNA translocating portal of the bacteriophage T4 packaging machine.Journal of molecular biology · 2014Article
- The C-terminal domain of the bacteriophage T4 terminase docks on the prohead portal clip region during DNA packaging.Virology · 2013Article
- Article
- Large terminase conformational change induced by connector binding in bacteriophage T7.The Journal of biological chemistry · 2013Article
- Function and horizontal transfer of the small terminase subunit of the tailed bacteriophage Sf6 DNA packaging nanomotor.Virology · 2013Article
- The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.Nucleic acids research · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
DNA packaging by double-stranded DNA bacteriophages and herpesviruses is driven by a powerful molecular machine assembled at the portal vertex of the empty prohead. The phage T4 packaging machine consists of three components: dodecameric portal (gp20), pentameric large terminase motor (gp17), and 11- or 12-meric small terminase (gp16). These components dynamically interact and orchestrate a complex series of reactions to produce a DNA-filled head containing one viral genome per head. Here, we analyzed the interactions between the portal and motor proteins using a direct binding assay, mutagenesis, and structural analyses. Our results show that a portal binding site is located in the ATP hydrolysis-controlling subdomain II of gp17. Mutations at key residues of this site lead to temperature-sensitive or null phenotypes. A conserved helix-turn-helix (HLH) that is part of this site interacts with the portal. A recombinant HLH peptide competes with gp17 for portal binding and blocks DNA translocation. The helices apparently provide specificity to capture the cognate prohead, whereas the loop residues communicate the portal interaction to the ATPase center. These observations lead to a hypothesis in which a unique HLH-portal interaction in the symmetrically mismatched complex acts as a lever to position the arginine finger and trigger ATP hydrolysis. Transiently connecting the critical parts of the motor; subdomain I (ATP binding), subdomain II (controlling ATP hydrolysis), and C-domain (DNA movement), the portal-motor interactions might ensure tight coupling between ATP hydrolysis and DNA translocation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.