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Article Dans Une Revue Nucleic Acids Research Année : 2013

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

Charlène Cornilleau
Noureddine Atmane
  • Fonction : Auteur
Eric Jacquet
Callum Smits
  • Fonction : Auteur
Juan C Alonso
  • Fonction : Auteur
Paulo Tavares
Leonor Oliveira
  • Fonction : Auteur
  • PersonId : 1312853

Résumé

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.

Domaines

Chimie organique

Dates et versions

hal-00778693 , version 1 (21-01-2013)

Identifiants

Citer

Charlène Cornilleau, Noureddine Atmane, Eric Jacquet, Callum Smits, Juan C Alonso, et al.. The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.. Nucleic Acids Research, 2013, 41 (1), pp.340-54. ⟨10.1093/nar/gks974⟩. ⟨hal-00778693⟩
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