ArticleThe Journal of biological chemistry2016
Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Something old, something new? Herpesvirus genome packaging examined in light of lessons from the tailed bacteriophages.Journal of virology · 2026Review
- Computational Investigation of Novel pUL56 Ligands Using Docking and Molecular Dynamics with Preliminary Cytotoxicity Evaluation: An Early-Stage Study.Molecules (Basel, Switzerland) · 2026Article
- Exploring EBNA3C Genetic Variability and Recombination in Epstein-Barr Virus-Associated Cancers.International journal of molecular sciences · 2026Article
- Isothermal Titration Calorimetry for Investigating Thermodynamics of Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Probing the extent of importin-α targeting of the TAF8 NLS by eliminating its cationic net-charge.Protein science : a publication of the Protein Society · 2025Article
- CanFrontiers in cellular and infection microbiology · 2025Article
- Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function.Viruses · 2022Review
- Differential recognition of canonical NF-κB dimers by Importin α3.Nature communications · 2022Article
- Pol α-primase dependent nuclear localization of the mammalian CST complex.Communications biology · 2021Article
- Structures and Divergent Mechanisms in Capsid Maturation and Stabilization Following Genome Packaging of Human Cytomegalovirus and Herpesviruses.Life (Basel, Switzerland) · 2021Review
- Evolutionary Selection of the Nuclear Localization Signal in the Viral Nucleoprotein Leads to Host Adaptation of the GenusViruses · 2020Article
- Review
- Experimental Dissection of the Lytic Replication Cycles of Herpes Simplex VirusesFrontiers in microbiology · 2018Review
- Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.PLoS pathogens · 2018Article
- Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin α isoforms.Scientific reports · 2017Article
- Mutual Interplay between the Human Cytomegalovirus Terminase Subunits pUL51, pUL56, and pUL89 Promotes Terminase Complex Formation.Journal of virology · 2017Article
- Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha.PloS one · 2017Article
- The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production.PLoS pathogens · 2016Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The tripartite terminase complex of herpesviruses assembles in the cytoplasm of infected cells and exploits the host nuclear import machinery to gain access to the nucleus, where capsid assembly and genome-packaging occur. Here we analyzed the structure and conservation of nuclear localization signal (NLS) sequences previously identified in herpes simplex virus 1 (HSV-1) large terminase and human cytomegalovirus (HCMV) small terminase. We found a monopartite NLS at the N terminus of large terminase, flanking the ATPase domain, that is conserved only in α-herpesviruses. In contrast, small terminase exposes a classical NLS at the far C terminus of its helical structure that is conserved only in two genera of the β-subfamily and absent in α- and γ-herpesviruses. In addition, we predicted a classical NLS in the third terminase subunit that is partially conserved among herpesviruses. Bioinformatic analysis revealed that both location and potency of NLSs in terminase subunits evolved more rapidly than the rest of the amino acid sequence despite the selective pressure to keep terminase gene products active and localized in the nucleus. We propose that swapping NLSs among terminase subunits is a regulatory mechanism that allows different herpesviruses to regulate the kinetics of terminase nuclear import, reflecting a mechanism of virus:host adaptation.
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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.