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Lookup NU author(s): Chrysoula Leontiou,
Professor Robert Lightowlers,
Professor Jeremy LakeyORCiD,
Professor Caroline AustinORCiD
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Topoisomerase IIβ binding to DNA has been analysed by surface plasmon resonance for the first time. Three DNA substrates with different secondary structures were studied, a 40 bp oligonucleotide, a four way junction and a 189 bp bent DNA fragment. We also compared the DNA binding kinetics of both human topoisomerase isoforms under identical conditions. Both α and β isoforms exhibited similar binding kinetics, with average equilibrium dissociation constants ranging between 1.4 and 2.9 nM. We therefore conclude that neither isoform has any preference for a specific DNA substrate under the conditions used in these experiments. © 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Author(s): Leontiou C, Lightowlers R, Lakey JH, Austin CA
Publication type: Article
Publication status: Published
Journal: FEBS Letters
ISSN (print): 0014-5793
ISSN (electronic): 1873-3468
PubMed id: 14596941
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