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Originally published In Press as doi:10.1074/jbc.C200550200 on November 21, 2002

J. Biol. Chem., Vol. 278, Issue 2, 1323-1327, January 10, 2003
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Functional Oligomeric State of Avian Sarcoma Virus Integrase*

Kogan K. BaoDagger , Hong Wang§, Jamie K. MillerDagger , Dorothy A. Erie§, Anna Marie Skalka, and Isaac WongDagger ||

From the Dagger  Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331, the § Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, and the  Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111

Retroviral integrase, one of only three enzymes encoded by the virus, catalyzes the essential step of inserting a DNA copy of the viral genome into the host during infection. Using the avian sarcoma virus integrase, we demonstrate that the enzyme functions as a tetramer. In presteady-state active site titrations, four integrase protomers were required for a single catalytic turnover. Volumetric determination of integrase-DNA complexes imaged by atomic force microscopy during the initial turnover additionally revealed substrate-induced assembly of a tetramer. These results suggest that tetramer formation may be a requisite step during catalysis with ramifications for antiviral design strategies targeting the structurally homologous human immunodeficiency virus, type 1 (HIV-1) integrase.

* This work was supported by National Institutes of Health Grant GM58771 (to I. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, Oregon State University, 2011 ALS Bldg., Corvallis, OR 97331. E-mail: wongis@onid.orst.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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