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.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Cornilleau C,Atmane N,Jacquet E,Smits C,Alonso JC,Tavares P,Oliveira Ldoi
10.1093/nar/gks974subject
Has Abstractpub_date
2013-01-07 00:00:00pages
340-54issue
1eissn
0305-1048issn
1362-4962pii
gks974journal_volume
41pub_type
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