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Kinetic analysis of human topoisomerase IIα and β DNA binding by surface plasmon resonance

Lookup NU author(s): Chrysoula Leontiou, Professor Robert Lightowlers, Professor Jeremy Lakey, Professor Caroline Austin

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Abstract

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.


Publication metadata

Author(s): Leontiou C, Lightowlers R, Lakey JH, Austin CA

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2003

Volume: 554

Issue: 1-2

Pages: 206-210

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: Elsevier

URL: http://dx.doi.org/10.1016/S0014-5793(03)01172-4

DOI: 10.1016/S0014-5793(03)01172-4

PubMed id: 14596941


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