ArticleJournal of virology2006
The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Something old, something new? Herpesvirus genome packaging examined in light of lessons from the tailed bacteriophages.Journal of virology · 2026Review
- Characterization of the Kaposi's sarcoma-associated herpesvirus terminase complex component ORF29.Microbiology spectrum · 2025Article
- Kaposi's Sarcoma-Associated Herpesvirus ORF67.5 Functions as a Component of the Terminase Complex.Journal of virology · 2023Article
- Kaposi's Sarcoma-Associated Herpesvirus ORF7 Is Essential for Virus Production.Microorganisms · 2021Article
- Role of the Herpes Simplex Virus CVSC Proteins at the Capsid Portal Vertex.Journal of virology · 2020Article
- Highlighting of a LAGLIDADG and a Zing Finger Motifs Located in the pUL56 Sequence Crucial for HCMV Replication.Viruses · 2019Article
- Review
- Sensitivity of the C-Terminal Nuclease Domain of Kaposi's Sarcoma-Associated Herpesvirus ORF29 to Two Classes of Active-Site Ligands.Antimicrobial agents and chemotherapy · 2018Article
- A Domain of Herpes Simplex Virus pUJournal of virology · 2017Article
- Mutual Interplay between the Human Cytomegalovirus Terminase Subunits pUL51, pUL56, and pUL89 Promotes Terminase Complex Formation.Journal of virology · 2017Article
- Herpesvirus Capsid Assembly and DNA Packaging.Advances in anatomy, embryology, and cell biology · 2017Review
- Development of Potent Antiviral Drugs Inspired by Viral Hexameric DNA-Packaging Motors with Revolving Mechanism.Journal of virology · 2016Review
- Intermolecular Complementation between Two Varicella-Zoster Virus pORF30 Terminase Domains Essential for DNA Encapsidation.Journal of virology · 2015Article
- Epstein-Barr virus BALF3 has nuclease activity and mediates mature virion production during the lytic cycle.Journal of virology · 2014Article
- Isolation and characterization of the herpes simplex virus 1 terminase complex.Journal of virology · 2014Article
- The structure of the herpes simplex virus DNA-packaging terminase pUL15 nuclease domain suggests an evolutionary lineage among eukaryotic and prokaryotic viruses.Journal of virology · 2013Article
- The human cytomegalovirus UL51 protein is essential for viral genome cleavage-packaging and interacts with the terminase subunits pUL56 and pUL89.Journal of virology · 2013Article
- Changes in subcellular localization reveal interactions between human cytomegalovirus terminase subunits.Virology journal · 2012Article
- Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex.Journal of proteome research · 2011Article
- A mutation in UL15 of herpes simplex virus 1 that reduces packaging of cleaved genomes.Journal of virology · 2011Article
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2 authors.
Funding
Abstract
Viral terminases play essential roles as components of molecular motors that package viral DNA into capsids. Previous results indicated that the putative terminase subunits of herpes simplex virus 1 (HSV-1) encoded by U(L)15 and U(L)28 (designated pU(L)15 and pU(L)28, respectively) coimmunoprecipitate with the U(L)33 protein from lysates of infected cells. All three proteins are among six required for HSV-1 DNA packaging but dispensable for assembly of immature capsids. The current results show that in both infected- and uninfected-cell lysates, pU(L)28 coimmunoprecipitates with either pU(L)33 or pU(L)15, whereas pU(L)15 and pU(L)33 do not coimmunoprecipitate unless pU(L)28 is present. The U(L)28 protein was sufficient to stabilize pU(L)33 from proteasomal degradation in an engineered cell line and was necessary to stabilize pU(L)33 in infected cells, whereas pU(L)15 had no such effects. The presence of pU(L)33 was dispensable for the pU(L)15/pU(L)28 interaction in lysates of both infected and uninfected cells but augmented the tendency for pU(L)15 and pU(L)28 to coimmunoprecipitate. These data suggest that pU(L)28 and pU(L)33 interact directly and that pU(L)15 interacts directly with pU(L)28 but only indirectly with pU(L)33. It is logical to propose that the indirect interaction of pU(L)15 and pU(L)33 is mediated through the interaction of both proteins with pU(L)28. The data also suggest that one function of pU(L)33 is to optimize the pU(L)15/pU(L)28 interaction.
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