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Papers In Press, published online ahead of print December 20, 2000
J. Biol. Chem, 10.1074/jbc.M009719200
Submitted on October 24, 2000
Revised on December 6, 2000
Accepted on December 19, 2000
Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854
Corresponding Author: brill{at}mbcl.rutgers.edu
Several members of the RecQ family of DNA helicases are known to interact with DNA topoisomerase III. Here we show that the S. cerevisiae Sgs1 and Top3 proteins physically interact in cell extracts and bind directly in vitro. Sgs1 and Top3 proteins co-immunoprecipitate from cell extracts under stringent conditions, indicating that Sgs1 and Top3 are present in a stable complex. The domain of Sgs1 that interacts with Top3 was identified by expressing Sgs1 truncations in yeast. The results indicate that the N-terminal 158 amino acids of Sgs1 are sufficient for the high affinity interaction between Sgs1 and Top3. In vitro assays using purified Top3 and N-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 N-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.
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