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J. Biol. Chem., Vol. 276, Issue 25, 22426-22438, June 22, 2001

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Characterization of Recombinant HPV6 and 11 E1 Helicases
EFFECT OF ATP ON THE INTERACTION OF E1 WITH E2 AND MAPPING OF A MINIMAL HELICASE DOMAIN^*

Peter W. White, Alex Pelletier, Karine Brault, Steve Titolo, Ewald Welchner, Louise Thauvette, Monika Fazekas, Michael G. Cordingley, and Jacques Archambault

From the Department of Biological Sciences, Boehringer Ingelheim (Canada) Ltd., Laval, Quebec H7S 2G5, Canada

To better characterize the enzymatic activities required for human papillomavirus (HPV) DNA replication, the E1 helicases of HPV types 6 and 11 were produced using a baculovirus expression system. The purified wild type proteins and a version of HPV11 E1 lacking the N-terminal 71 amino acids, which was better expressed, were found to be hexameric over a wide range of concentrations and to have helicase and ATPase activities with relatively low values for K_m(ATP) of 12 µM for HPV6 E1 and 6 µM for HPV11 E1. Interestingly, the value of K_m(ATP) was increased 7-fold in the presence of the E2 transactivation domain. In turn, ATP was found to perturb the co-operative binding of E1 and E2 to DNA. Mutant and truncated versions of in vitro translated E1 were used to identify a minimal ATPase domain composed of the C-terminal 297 amino acids. This fragment was expressed, purified, and found to be fully active in ATP hydrolysis, single-stranded DNA binding, and unwinding assays, despite lacking the minimal origin-binding domain.

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