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Nucleic Acids Research, 1993, Vol. 21, No. 8 1697-1704
© 1993

ENZYMOLOGY

Topoisomerase activity is associated with purified SV40 T antigen

Kristine Mann

Biology Department, University of Alaska AK 99508, USA

Received March 18, 1993. Accepted March 18, 1993.

Purified SV40 T antigen has been assayed for topolsomerase activity. The ability to relax negatlvely-supercolled SV40 DNA was found In preparations of T antigen purified either from human 293 cells Infected with Ad5-SVR111 virus or from insect Sf9 cells Infected with recombinant baculovlrus 941T. The T antigen-associated relaxing activity was stimulated by MgCl2 and was not dependent on ATP, suggesting that it is not due to cellular topoisomerase II. The topoisomerase activity was immunopreclpltated by a monoclonal antibody specific for T antigen, but not by a control monoclonal antibody. In addition, Immunoblottlng of purified T antigen from human 293 cells with anti-human topoisomerase I and anti-human topoisomerase II antibodies failed to detect cellular topoisomerases I or II. Sedimentation analysis of purified T antigen revealed that the topoisomerase activity co-sedlmented with the hexameric form of T antigen at 23S. The topoisomerase activity is, therefore, either Inherent to T antigen or due to a cellular topoisomerase I tightly bound to, and co-purifying with, T antigen.


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