Abstract
A 17-amino-acid residue domain has been identified in Escherichia coli DNA topoisomerase II (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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 888-895 |
| Number of pages | 8 |
| Journal | Molecular Microbiology |
| Volume | 35 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2000 |
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