The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.

doi:10.1093/nar/gks974

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Article

The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.

Nucleic acids research - 7 Jan 2013

Cornilleau Charlène, Atmane Noureddine, Jacquet Eric, Smits Callum, Alonso Juan C, Tavares Paulo, Oliveira Leonor

Abstract excerpt

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...

Topics

Adenosine Triphosphatases
Bacillus Phages
Capsid
Catalytic Domain
Cations, Divalent
DNA Cleavage
DNA Packaging
Endodeoxyribonucleases
Manganese
Metals
Mutation
Phenotype
Protein Structure, Tertiary
Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 23118480
DOI: 10.1093/nar/gks974
PMCID: PMC3592435

Genes

SPP1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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