<p>DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks [<cite idref="PUB00005437"/>]. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis [<cite idref="PUB00020794"/>, <cite idref="PUB00016842"/>]. DNA topoisomerases are divided into two classes: type I enzymes (<db_xref db="EC" dbkey="5.99.1.2"/>; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (<db_xref db="EC" dbkey="5.99.1.3"/>; topoisomerases II, IV and VI) break double-strand DNA [<cite idref="PUB00020793"/>].</p><p>Type I topoisomerases are ATP-independent enzymes (except for reverse gyrase), and can be subdivided according to their structure and reaction mechanisms: type IA (bacterial and archaeal topoisomerase I, topoisomerase III and reverse gyrase) and type IB (eukaryotic topoisomerase I and topoisomerase V). These enzymes are primarily responsible for relaxing positively and/or negatively supercoiled DNA, except for reverse gyrase, which can introduce positive supercoils into DNA. </p><p>This entry describes topoisomerase III from bacteria and its equivalent encoded on plasmids. In <taxon tax_id="562">Escherichia coli</taxon>, topoisomerase III functions as the principal cellular decatenase, capable of unlinking replicating daughter chromosomes [<cite idref="PUB00020797"/>]. Topoisomerase III requires single-stranded DNA for binding, so it is more efficient at decatenating chromosomes if the DNA circles contain a small gap. It appears that Topoisomerase III works by removing precatenanes, an alternative form that can be taken by the positive linkages that arise between the daughter chromosomes during replication. Topoisomerase III shows considerable identity to bacterial topoisomerase I, except that it lacks the zinc finger region found in the latter.</p><p>More information about this protein can be found at Protein of the Month: DNA Topoisomerase [<cite idref="PUB00035961"/>].</p> DNA topoisomerase III, bacterial-type