Nucleic Acids Research, Vol 25, Issue 3 604-611, Copyright © 1997 by Oxford University Press
H Gmunder, K Kuratli and W Keck
A key step in the supercoiling reaction is the DNA gyrase-mediated cleavage
and religation step of double-stranded DNA. Footprinting studies suggest
that the DNA gyrase binding site is 100-150 bp long and that the DNA is
wrapped around the enzyme with the cleavage site located near the center of
the fragment. Subunit A inhibitors interrupt this cleavage and resealing
cycle and result in cleavage occurring at preferred sites. We have been
able to show that even a 30 bp DNA fragment containing a 20 bp preferred
cleavage sequence from the pBR322 plasmid was a substrate for the DNA
gyrase-mediated cleavage reaction in the presence of inhibitors. This DNA
fragment was cleaved, although with reduced efficiency, at the same sites
as a 122 bp DNA fragment. A 20 bp DNA fragment was cleaved with low
efficiency at one of these sites and a 10 bp DNA fragment was no longer a
substrate. We therefore propose that subunit A inhibitors interact with DNA
at inhibitor- specific positions, thus determining cleavage sites by
forming ternary complexes between DNA, inhibitors and DNA gyrase.
ARTICLES
In the presence of subunit A inhibitors DNA gyrase cleaves DNA fragments as short as 20 bp at specific sites
F. Hoffmann-La Roche Ltd, Pharmaceutical Research Preclinical Infectious Diseases, CH-4070 Basel, Switzerland. hans.gmuender@roche.com
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