Mapping of the Interaction Domain of DNA Topoisomerase $II{\alpha}$ and $II{\beta}$ with Extracellular Signal-Regulated Kinase 2

  • Park, Gye-Hwa (Department of Biochemistry, College of Natural Sciences, Kyungpook National University) ;
  • Bae, Young-Seuk (Department of Biochemistry, College of Natural Sciences, Kyungpook National University)
  • Received : 2000.10.30
  • Accepted : 2000.11.27
  • Published : 2001.01.31

Abstract

Both topoisomerase $II{\alpha}$ and $II{\beta}$ east as phosphoproteins in the cells. Recently it was reported that DNA topoisomerase $II{\alpha}$ associates with and is phosphorylated by the extracellular signal-regulated kinase 2 (ERK2). Also, ERK2 stimulates the activity of topoisomerase II by a phosphorylation-independent manner [Shapiro et al., (1999) Mol. Cell. Biol. 19, 3551-3560]. In this study, a yeast two-hybrid system was used to investigate the binding site between topoisomerase $II{\alpha}$ or $II{\beta}$ and ERK2. The two-hybrid test clearly showed that topoisomerase $II{\beta}$ residues 1099-1263, and topoisomerase $II{\alpha}$ residues 1078-1182, mediate the interaction with ERK2, and that the leucine zipper motifs of topoisomerase $II{\alpha}$ and $II{\beta}$ are not required for its physical binding to ERK2. Our results suggest that topoisomerase $II{\beta}$ residues 1099-1263, and topoisomerase $II{\alpha}$ residues 1078-1182, may be common binding sites for activator proteins.

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