4.5 Article

Identification of a unique domain essential for Escherichia coli DNA topoisomerase III-catalysed decatenation of replication intermediates

Journal

MOLECULAR MICROBIOLOGY
Volume 35, Issue 4, Pages 888-895

Publisher

BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1365-2958.2000.01763.x

Keywords

-

Funding

  1. NIGMS NIH HHS [GM48445, GM34558, GM51350, R01 GM051350] Funding Source: Medline

Ask authors/readers for more resources

A 17-amino-acid residue domain has been identified in Escherichia coli DNA topoisomerase III (Topo III) that is essential for Topo III-mediated resolution of DNA replication intermediates in vitro. Deletion of this domain reduced Topo III-catalysed resolution of DNA replication intermediates and decatenation of multiply linked plasmid DNA dimers by four orders of magnitude, whereas reducing Topo III-catalysed relaxation of negatively supercoiled DNA substrates only 20-fold. The presence of this domain has been detected in multiple plasmid-encoded topoisomerases, raising the possibility that these enzymes may also be decatenases.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available