Abstract
Topoisomerase II (topo II) catalyzes the decatenation of interlinked DNA molecules and is essential for chromosome segregation. To test the hypothesis that the noncatalytic C-terminal domain of topo II is necessary for mediating interactions with other proteins required for chromosome segregation, we used a two-hybrid cloning strategy to identify proteins that interact with S. cerevisiae topo II in vivo. One protein identified (Sgs1p) is structurally related to E. coli RecQ protein and contains helicase signature motifs. Strains lacking Sgs1p exhibit elevated levels of chromosome missegregation during both mitotic and meiotic division. We propose a model to account for the interaction of a toposomerase and a helicase in the faithful segregation of newly replicated eukaryotic chromosomes.
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