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Nucleic Acids Research, 1985, Vol. 13, No. 5 1543-1557
© 1985

Articles

Topoisomerase I has a strong binding preference for a conserved hexadecameric sequence in the promotor region of the rRNA gene from Tetrahymena pyriformis

Anni H. Andersen, Elmar Gocke, Bjarne J. Bonven, Ole F. Nielsen and Ole Westergaard

Department of Molecular Biology and Plant Physiology, University of Aarhus C.F.Møllers Allé 130, DK-8000 Århus C, Denmark

Received December 12, 1984. Revised February 6, 1985. Accepted February 6, 1985.

Topoisomerase I is in situ associated with DNaseI hypersensitive sites located in the promotor and terminator regions of the extrachromosomal rDNA in Tetrahymena thermophila at sites with sequences fitting the motif Formula . Reconstitution experiments with purified topoisomerase I and cloned fragments of rDNA demonstrate that the enzyme exhibits the same binding and cleavage properties on naked DNA. These observations are striking as topoisomerase I previously has been found to exhibit low sequence specificity. The specific binding of the enzyme has an absolute requirement for divalent cations with a preference for Ca2+. The strong binding to the hexadecamer has been characterized by competition experiments, and it has been used to determine the molecular weight of the enzyme.


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