ArticleNucleic acids research2017
The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 50 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Expanding the DNA damaging potential of artificial metallo-nucleases with click chemistry.Nature communications · 2026Article
- Duck Plague Virus Full-Length UL15 Protein Is a Multifunctional Enzyme Which Not Only Possesses Nuclease Activity but Also Exerts ATPase and DNA-Binding Activity.Veterinary sciences · 2025Article
- Characterization and genomic analysis of twoFrontiers in microbiology · 2025Article
- Complementary insights into gut viral genomes: a comparative benchmark of short- and long-read metagenomes using diverse assemblers and binners.Microbiome · 2024Article
- Origin, Evolution and Diversity of φ29-like Phages-Review and Bioinformatic Analysis.International journal of molecular sciences · 2024Review
- Article
- Mechanism of Viral DNA Packaging in Phage T4 Using Single-Molecule Fluorescence Approaches.Viruses · 2024Review
- Viral Genomic DNA Packaging Machinery.Sub-cellular biochemistry · 2024Review
- Insights into a viral motor: the structure of the HK97 packaging termination assembly.Nucleic acids research · 2023Article
- Review
- Use of an Integrated Approach Involving AlphaFold Predictions for the Evolutionary Taxonomy ofBiomolecules · 2023Article
- Article
- Terminase Subunits from the Pseudomonas-Phage E217.Journal of molecular biology · 2022Article
- Viral Small Terminase: A Divergent Structural Framework for a Conserved Biological Function.Viruses · 2022Review
- Molecular dynamics of DNA translocation by FtsK.Nucleic acids research · 2022Article
- Article
- Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.Nucleic acids research · 2021Article
- Viral packaging ATPases utilize a glutamate switch to couple ATPase activity and DNA translocation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Biophysical analysis of Pseudomonas-phage PaP3 small terminase suggests a mechanism for sequence-specific DNA-binding by lateral interdigitation.Nucleic acids research · 2020Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many viruses use a powerful terminase motor to pump their genome inside an empty procapsid shell during virus maturation. The large terminase (TerL) protein contains both enzymatic activities necessary for packaging in such viruses: the adenosine triphosphatase (ATPase) that powers DNA translocation and an endonuclease that cleaves the concatemeric genome at both initiation and completion of genome packaging. However, how TerL binds DNA during translocation and cleavage remains mysterious. Here we investigate DNA binding and cleavage using TerL from the thermophilic phage P74-26. We report the structure of the P74-26 TerL nuclease domain, which allows us to model DNA binding in the nuclease active site. We screened a large panel of TerL variants for defects in binding and DNA cleavage, revealing that the ATPase domain is the primary site for DNA binding, and is required for nuclease activity. The nuclease domain is dispensable for DNA binding but residues lining the active site guide DNA for cleavage. Kinetic analysis of DNA cleavage suggests flexible tethering of the nuclease domains during DNA cleavage. We propose that interactions with the procapsid during DNA translocation conformationally restrict the nuclease domain, inhibiting cleavage; TerL release from the capsid upon completion of packaging unlocks the nuclease domains to cleave DNA.
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