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Kinetic analysis of human topoisomerase IIα and β DNA binding by surface plasmon resonance
Author(s) -
Leontiou Chrysoula,
Lightowlers Robert,
Lakey Jeremy H.,
Austin Caroline A.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01172-4
Subject(s) - surface plasmon resonance , topoisomerase , biophysics , dna , chemistry , surface plasmon , nuclear magnetic resonance , biochemistry , plasmon , materials science , nanotechnology , biology , physics , optoelectronics , nanoparticle
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.