ArticleNucleic acids research2013
The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 30 citations in OpenAlex.
- Dissecting the dsDNA viral packaging machinery: structural evolution and potential for therapeutics.Journal of virology · 2026Review
- Article
- Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.Nucleic acids research · 2017Article
- Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.Nucleic acids research · 2015Article
- Mechanisms of DNA Packaging by Large Double-Stranded DNA Viruses.Annual review of virology · 2015Review
- Virus evolution toward limited dependence on nonessential functions of the host: the case of bacteriophage SPP1.Journal of virology · 2015Article
- Ligand induced stabilization of the melting temperature of the HSV-1 single-strand DNA binding protein using the thermal shift assay.Biochemical and biophysical research communications · 2014Article
- Staphylococcal pathogenicity island DNA packaging system involving cos-site packaging and phage-encoded HNH endonucleases.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure-function analysis of the DNA translocating portal of the bacteriophage T4 packaging machine.Journal of molecular biology · 2014Article
- The C-terminal domain of the bacteriophage T4 terminase docks on the prohead portal clip region during DNA packaging.Virology · 2013Article
- Dualities in the analysis of phage DNA packaging motors.Bacteriophage · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The large terminase subunit is a central component of the genome packaging motor from tailed bacteriophages and herpes viruses. This two-domain enzyme has an N-terminal ATPase activity that fuels DNA translocation during packaging and a C-terminal nuclease activity required for initiation and termination of the packaging cycle. Here, we report that bacteriophage SPP1 large terminase (gp2) is a metal-dependent nuclease whose stability and activity are strongly and preferentially enhanced by Mn(2+) ions. Mutation of conserved residues that coordinate Mn(2+) ions in the nuclease catalytic site affect the metal-induced gp2 stabilization and impair both gp2-specific cleavage at the packaging initiation site pac and unspecific nuclease activity. Several of these mutations block also DNA encapsidation without affecting ATP hydrolysis or gp2 C-terminus binding to the procapsid portal vertex. The data are consistent with a mechanism in which the nuclease domain bound to the portal switches between nuclease activity and a coordinated action with the ATPase domain for DNA translocation. This switch of activities of the nuclease domain is critical to achieve the viral chromosome packaging cycle.
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