ArticleJournal of virology2010
Vaccinia virus D4 mutants defective in processive DNA synthesis retain binding to A20 and DNA.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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
22 citing papers in PubMed, 28 citations in OpenAlex.
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- Identification of core therapeutic targets for Monkeypox virus and repurposing potential of drugs: A WEB prediction approach.PloS one · 2024Article
- Correlated Target Search by Vaccinia Virus Uracil-DNA Glycosylase, a DNA Repair Enzyme and a Processivity Factor of Viral Replication Machinery.International journal of molecular sciences · 2023Article
- Structural basis for the assembly of the DNA polymerase holoenzyme from a monkeypox virus variant.Science advances · 2023Article
- A small molecule that targets the processivity factor of molluscum contagiosum virus has therapeutic potential.Antiviral research · 2023Article
- Herpes Simplex Virus-1 infection in human primary corneal epithelial cells is blocked by a stapled peptide that targets processive DNA synthesis.The ocular surface · 2021Article
- Inhibitors of DNA Glycosylases as Prospective Drugs.International journal of molecular sciences · 2020Review
- Mutation and structure guided discovery of an antiviral small molecule that mimics an essential C-Terminal tripeptide of the vaccinia D4 processivity factor.Antiviral research · 2019Article
- The vaccinia virus DNA polymerase and its processivity factor.Virus research · 2017Review
- A Conserved Tripeptide Sequence at the C Terminus of the Poxvirus DNA Processivity Factor D4 Is Essential for Protein Integrity and Function.The Journal of biological chemistry · 2016Article
- Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases.Protein science : a publication of the Protein Society · 2016Review
- Crystal Structure of the Vaccinia Virus Uracil-DNA Glycosylase in Complex with DNA.The Journal of biological chemistry · 2015Article
- Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase.BMC structural biology · 2015Article
- A novel target and approach for identifying antivirals against molluscum contagiosum virus.Antimicrobial agents and chemotherapy · 2014Article
- Uracil-DNA glycosylases-structural and functional perspectives on an essential family of DNA repair enzymes.Protein science : a publication of the Protein Society · 2014Review
- Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminal domain.PLoS pathogens · 2014Article
- Design of potent poxvirus inhibitors of the heterodimeric processivity factor required for viral replication.Journal of medicinal chemistry · 2013Article
- Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Identification of protein-protein interaction inhibitors targeting vaccinia virus processivity factor for development of antiviral agents.Antimicrobial agents and chemotherapy · 2011Article
- Computational analysis of DNA replicases in double-stranded DNA viruses: relationship with the genome size.Nucleic acids research · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Genome replication is inefficient without processivity factors, which tether DNA polymerases to their templates. The vaccinia virus DNA polymerase E9 requires two viral proteins, A20 and D4, for processive DNA synthesis, yet the mechanism of how this tricomplex functions is unknown. This study confirms that these three proteins are necessary and sufficient for processivity, and it focuses on the role of D4, which also functions as a uracil DNA glycosylase (UDG) repair enzyme. A series of D4 mutants was generated to discover which sites are important for processivity. Three point mutants (K126V, K160V, and R187V) which did not function in processive DNA synthesis, though they retained UDG catalytic activity, were identified. The mutants were able to compete with wild-type D4 in processivity assays and retained binding to both A20 and DNA. The crystal structure of R187V was resolved and revealed that the local charge distribution around the substituted residue is altered. However, the mutant protein was shown to have no major structural distortions. This suggests that the positive charges of residues 126, 160, and 187 are required for D4 to function in processive DNA synthesis. Consistent with this is the ability of the conserved mutant K126R to function in processivity. These mutants may help unlock the mechanism by which D4 contributes to processive DNA synthesis.
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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.