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M603314200v1
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Papers In Press, published online ahead of print May 30, 2006
J. Biol. Chem, 10.1074/jbc.M603314200
Submitted on April 6, 2006
Revised on May 23, 2006
Accepted on May 30, 2006

Modulation of the viral ATPase activity by the portal protein correlates with DNA packaging efficiency

Leonor Oliveira, Adriano O. Henriques, and Paulo Tavares

Unité de Virologie Moléculaire et Structurale, Centre National de la Recherche Scientifique, Gif-sur-Yvette 91198

Corresponding Author: oliveira{at}vms.cnrs-gif.fr

DNA packaging in tailed bacteriophages and herpes viruses requires assembly of a complex molecular machine at a specific vertex of a preformed procapsid. Like in all these viruses, the DNA translocation motor of bacteriophage SPP1 is composed of the portal protein (gp6) that provides a tunnel for DNA entry into the procapsid and of the viral ATPase (gp1-gp2 complex) that fuels DNA translocation. Here we studied the cross-talk between the components of the motor to control its ATP consumption and DNA encapsidation. We showed that gp6 embedded in the procapsid structure stimulated more than 10-fold the gp2 ATPase activity. This stimulation, that was significantly higher than the one conferred by isolated gp6, depended on the presence of gp1. Mutations in different regions of gp6 abolished or decreased the gp6-induced stimulation of the ATPase. This effect on gp2 activity was observed both in the presence and in the absence of DNA and showed a strict correlation with the efficiency of DNA packaging into procapsids containing the mutant portals. Our results demonstrated that the portal protein has an active control over the viral ATPase activity that correlates with the performance of the DNA packaging motor.


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