Characterization of topoisomerase II-DNA interaction and identification of a DNA-binding domain by ultraviolet laser crosslinking.

Abstract:

:We have used ultraviolet laser crosslinking to characterize the DNA-binding properties of highly purified yeast topoisomerase II in the absence of ATP. A single 5 ns, 20 mJ pulse of 266 nm light produced optimal crosslinking to a short DNA duplex, with an efficiency of 0.25%. An equilibrium binding constant (Keq) of 1.2 +/- 0.5 x 10(8) M(-1) was determined from kinetic analysis. Topoisomerase II showed highest affinity for supercoiled DNA. Limited proteolysis of crosslinked topoisomerase II-DNA complexes showed a site of crosslinking to be within a 29-kDa fragment with Leu-681 at its amino-terminal end. This region contains the active Tyr-783 and is homologous to the amino-terminal region of the DNA-binding bacterial gyrase GyrA subunit, suggesting a conserved DNA-binding mechanism.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hung F,Luo D,Sauvé DM,Muller MT,Roberge M

doi

10.1016/0014-5793(96)00035-x

subject

Has Abstract

pub_date

1996-02-12 00:00:00

pages

127-32

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00035-X

journal_volume

380

pub_type

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