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C200550200v1
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Papers In Press, published online ahead of print November 21, 2002
J. Biol. Chem, 10.1074/jbc.C200550200
Submitted on September 27, 2002
Revised on November 7, 2002
Accepted on November 21, 2002

Functional oligomeric state of avian sarcoma virus integrase

Kogan K. Bao, Hong Wang, Jamie K. Miller, Dorothy A. Erie, Anna M. Skalka, and Isaac Wong

Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331

Corresponding Author: wongis{at}onid.orst.edu

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.


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