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DNA topoisomerase IV is a bacterial type II topoisomerase enzyme that plays a critical role in managing the topology of bacterial chromosomes during replication and cell division. Its primary function is to unlink (decatenate) interlinked daughter chromosomes following DNA replication, ensuring proper chromosome segregation. It also relaxes positive supercoils ahead of the replication fork. Topoisomerase IV is an important antibacterial drug target, with quinolone antibiotics inhibiting the enzyme by stabilizing the transient cleavage complex.
Stabilization of the transient cleavage complex formed between enzyme and DNA, leading to lethal double-strand breaks.
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