ArticleThe Journal of biological chemistry2015
Crystal Structure of the Vaccinia Virus Uracil-DNA Glycosylase in Complex with DNA.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Single-Cell Transcriptomic Changes in Patient-Derived Glioma and U87 Glioblastoma Cell Cultures Infected with the Oncolytic Virus VV-GMCSF-Lact.International journal of molecular sciences · 2025Article
- Structural basis of DNA replication fidelity of the Mpox virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Programmable DNA pyrimidine base editing via engineered uracil-DNA glycosylase.Nature communications · 2024Article
- Structural insight into the assembly and working mechanism of helicase-primase D5 from Mpox virus.Nature structural & molecular biology · 2024Article
- Missing subunits of Mpox replication complex: Possible impact on structural organization.The Journal of infection · 2023Article
- 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 New Class of Uracil-DNA Glycosylase Inhibitors Active against Human and Vaccinia Virus Enzyme.Molecules (Basel, Switzerland) · 2021Article
- Contribution of the French army health service in support of expertise and research in infectiology in Africa.New microbes and new infections · 2018Article
- The French Armed Forces Virology Unit: A Chronological Record of Ongoing Research on Orthopoxvirus.Viruses · 2017Review
- The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.Nature communications · 2017Article
- Identification of Vaccinia Virus Replisome and Transcriptome Proteins by Isolation of Proteins on Nascent DNA Coupled with Mass Spectrometry.Journal of virology · 2017Article
- Uracil DNA glycosylase (UDG) activities in Bradyrhizobium diazoefficiens: characterization of a new class of UDG with broad substrate specificity.Nucleic acids research · 2017Article
- 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
- Domain Organization of Vaccinia Virus Helicase-Primase D5.Journal of virology · 2016Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vaccinia virus polymerase holoenzyme is composed of the DNA polymerase catalytic subunit E9 associated with its heterodimeric co-factor A20·D4 required for processive genome synthesis. Although A20 has no known enzymatic activity, D4 is an active uracil-DNA glycosylase (UNG). The presence of a repair enzyme as a component of the viral replication machinery suggests that, for poxviruses, DNA synthesis and base excision repair is coupled. We present the 2.7 Å crystal structure of the complex formed by D4 and the first 50 amino acids of A20 (D4·A201-50) bound to a 10-mer DNA duplex containing an abasic site resulting from the cleavage of a uracil base. Comparison of the viral complex with its human counterpart revealed major divergences in the contacts between protein and DNA and in the enzyme orientation on the DNA. However, the conformation of the dsDNA within both structures is very similar, suggesting a dominant role of the DNA conformation for UNG function. In contrast to human UNG, D4 appears rigid, and we do not observe a conformational change upon DNA binding. We also studied the interaction of D4·A201-50 with different DNA oligomers by surface plasmon resonance. D4 binds weakly to nonspecific DNA and to uracil-containing substrates but binds abasic sites with a Kd of <1.4 μm. This second DNA complex structure of a family I UNG gives new insight into the role of D4 as a co-factor of vaccinia virus DNA polymerase and allows a better understanding of the structural determinants required for UNG action.
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