Escherichia coli DNA topoisomerase III is a site-specific DNA binding protein that binds asymmetrically to its cleavage site

25Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

The binding of DNA topoisomerase III (Tope III) to a single-stranded DNA substrate containing a strong cleavage site has been examined. The minimal substrate requirement for Tope III-catalyzed cleavage has been determined to consist of 7 bases: 6 bases 5' to the cleavage site and only 1 base 3' to the site. Nuclease P1 protection experiments indicate that the enzyme also binds to its substrate asymmetrically, protecting ~ 12 bases 5' to the cleavage site and only 2 bases 3' to the cleavage site, A catalytically inactive mutant of Tope III shows the same protection pattern as the active polypeptide, indicating that Tope III is a site-specific binding protein as well as a topoisomerase. Consistent with this view, an oligonucleotide containing a cleavage site is a more effective inhibitor and is bound more efficiently by Tope III than an oligonucleotide without a cleavage site.

Cite

CITATION STYLE

APA

Zhang, H. L., Malpure, S., & DiGate, R. J. (1995). Escherichia coli DNA topoisomerase III is a site-specific DNA binding protein that binds asymmetrically to its cleavage site. Journal of Biological Chemistry, 270(40), 23700–23705. https://doi.org/10.1074/jbc.270.40.23700

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free