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DNA-independent ATPase activity of the Trichoplusia ni granulovirus DNA helicase

Graduate Program in Genetics¹ and Department of Entomology², University of California, Riverside, CA 92521, USA

Author for correspondence: Brian Federici (at Department of Entomology). Fax +1 909 787 3086 or 3681. e-mail brian.federici{at}ucr.edu

DNA helicases of baculoviruses are essential for virus replication and have been implicated as molecular determinants of host range. Although these proteins contain seven motifs (I, Ia, II–VI) characteristic of DNA helicases, the two most important characteristics of helicases – duplex-DNA unwinding and ATPase activity – have not been demonstrated. In the present study, a recombinant putative DNA helicase (rP137) of Trichoplusia ni granulovirus (TnGV) was purified from insect cells infected with a recombinant Autographa californica multicapsid nucleopolyhedrovirus that overproduced rP137. The rP137 protein exhibited an intrinsic DNA-independent ATPase activity that required Mg²⁺ as a co-factor, an activity that was reduced in the presence of TnGV and phage DNAs. These results provide further evidence that baculovirus helicase genes encode proteins with biochemical properties similar to those of classical DNA helicases.

This article has been cited by other articles:

				D. K. Bideshi and B. A. Federici The Trichoplusia ni granulovirus helicase is unable to support replication of Autographa californica multicapsid nucleopolyhedrovirus in cells and larvae of T. ni J. Gen. Virol., June 1, 2000; 81(6): 1593 - 1599. [Abstract] [Full Text]