Nucleic Acids Research, 1991, Vol. 19, No. 6 1235-1241
© 1991
MOLECULAR BIOLOGY |
Eukaryotic topoisomerase I-DNA interaction is stabilized by helix curvature
Department of Molecular Biology and Plant Physiology, Universfty of Aarhus C.F.Møllers Allé 130, 8000 Aarhus C, Denmark
* To whom correspondence should be addressed
Received December 28, 1990. Revised February 27, 1991. Accepted February 27, 1991.
The influence of DNA structure on topoisomerase I- DNA interaction has been investigated using a high affinity binding site and mutant derivatives thereof. Parallel determinations of complex formation and helix structure in the absence of superhelical stress suggest that the interaction is intensified by stable helix curvature. Previous work showed that a topoisomerase I binding site consists of two functionally distinct subdomains. A region located 5' to the topolsomerase I cleavage site is essential for binding. The region 3' to the cleavage site is covered by the enzyme, but not essential. We report here that the helix conformation of the latter region is an important modulator of complex formation. Thus, complex formation is markedly stimulated, when an intrinsically bent DNA segment is installed in this region. A unique pattern of phosphate ethylatlon Interferences in the 3'-part of the binding site indicates that sensing of curvature involves backbone contacts. Since dynamic curvature in supercoiled DNA may substitute for stable curvature, our findings suggest that topoisomerase I is able to probe DNA topology by assessment of writhe, rather than twist.
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