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 Lettjournal_title
FEBS lettersauthors
Hung F,Luo D,Sauvé DM,Muller MT,Roberge Mdoi
10.1016/0014-5793(96)00035-xsubject
Has Abstractpub_date
1996-02-12 00:00:00pages
127-32issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(96)00035-Xjournal_volume
380pub_type
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