Journal
MOLECULAR MICROBIOLOGY
Volume 35, Issue 4, Pages 888-895Publisher
BLACKWELL SCIENCE LTD
DOI: 10.1046/j.1365-2958.2000.01763.x
Keywords
-
Categories
Funding
- 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
Recommended
No Data Available