Table 1.
Classification of topoisomerases
| Type | Polarity | Mechanism | Humans | Bacteria | ||||
|---|---|---|---|---|---|---|---|---|
| Genes | Proteins | Drugs | Genes | Proteins | Drugs | |||
| IA | 5'-PY | Strand passage | TOP3A | Top3α | none | TOPA | Topo I | none |
| TOP3B | Top3β | none | TOPB | Topo III | none | |||
| IB | 3'-PY | Rotation | TOP1 | Top1 | anticancer | usually | ||
| TOP1MT | Top1mt | none (?) | none | |||||
| GYRA | Gyrase | |||||||
| TOP2A | Top2α | GYRB | ||||||
| IIA | 5'-PY | Strand passage | anticancer | Antibiotics | ||||
| ATPase | TOP2B | Top2β | PARC | Topo IV | ||||
| PARE | ||||||||
Type I enzymes are monomeric and cleave one strand of DNA for catalysis. Type II enzymes are homodimeric (humans) or heterotetrameric (bacteria), and cleave both strands of duplex DNA with a 5’-four-base overhang (see Fig. 2).