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Originally published In Press as doi:10.1074/jbc.M009719200 on December 20, 2000

J. Biol. Chem., Vol. 276, Issue 12, 8848-8855, March 23, 2001
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Mapping the DNA Topoisomerase III Binding Domain of the Sgs1 DNA Helicase*

William M. Fricke, Vivek Kaliraman, and Steven J. BrillDagger

From the Department of Molecular Biology and Biochemistry, Center for Advanced Biotechnology and Medicine, Rutgers University, Piscataway, New Jersey 08855

Several members of the RecQ family of DNA helicases are known to interact with DNA topoisomerase III (Top3). Here we show that the Saccharomyces cerevisiae Sgs1 and Top3 proteins physically interact in cell extracts and bind directly in vitro. Sgs1 and Top3 proteins coimmunoprecipitate from cell extracts under stringent conditions, indicating that Sgs1 and Top3 are present in a stable complex. The domain of Sgs1 which interacts with Top3 was identified by expressing Sgs1 truncations in yeast. The results indicate that the NH2-terminal 158 amino acids of Sgs1 are sufficient for the high affinity interaction between Sgs1 and Top3. In vitro assays using purified Top3 and NH2-terminal Sgs1 fragments demonstrate that at least part of the interaction is through direct protein-protein interactions with these 158 amino acids. Consistent with these physical data, we find that mutant phenotypes caused by a point mutation or small deletions in the Sgs1 NH2 terminus can be suppressed by Top3 overexpression. We conclude that Sgs1 and Top3 form a tight complex in vivo and that the first 158 amino acids of Sgs1 are necessary and sufficient for this interaction. Thus, a primary role of the Sgs1 amino terminus is to mediate the Top3 interaction.

* This work was supported by National Institutes of Health Grants GM55583 and AG16637.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.

Dagger To whom correspondence should be addressed: Dept. of Molecular Biology and Biochemistry, Center for Advanced Biotechnology and Medicine, 679 Hoes Lane, Rutgers University, Piscataway, NJ 08854. Tel.: 732-235-4197; Fax: 732-235-4880; E-mail: brill@mbcl.rutgers.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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