DNA Topoisomerase Activity in Cellular Mechanisms
Summary
DNA topoisomerases are essential enzymes that regulate the topology of the genome by introducing transient breaks in one or both strands of the DNA helix. These enzymes relieve torsional stress generated during replication, transcription and chromosome segregation by catalysing controlled strand passage and resealing reactions. Type I topoisomerases cleave a single DNA strand to permit rotation and relaxation of supercoils, whereas type II topoisomerases transiently break both strands to effect decatenation, unknotting and the removal or introduction of superhelical turns in an ATP-dependent manner. Through these activities, topoisomerases ensure faithful DNA duplication, maintain genomic stability and facilitate chromatin remodelling. Dysregulation or inhibition of topoisomerase function underpins the action of various antibacterial and anticancer agents, while mutations in topoisomerase genes have been linked to developmental disorders and neurodegeneration. Recent advances have elucidated structural details of the catalytic cycle, revealed non-canonical roles in transcriptional regulation and highlighted the potential for selective targeting in parasitic and thermophilic organisms.
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Technical terms
Supercoiling: The over- or under-twisting of the DNA double helix, generating torsional strain that must be resolved for replication and transcription to proceed.
Type I topoisomerase: An enzyme that cleaves one strand of a DNA duplex, allowing unidirectional rotation of the broken ends to relax supercoils without requiring ATP.
Type II topoisomerase: An ATP-dependent enzyme that transiently cleaves both strands of DNA to manage catenanes, knots and superhelical tension, crucial for chromosome segregation.
Cleavable complex: A transient covalent intermediate formed when a topoisomerase is linked to DNA via phosphotyrosine bonds during the strand-breakage and reunion cycle.
Decatenation: The enzymatic process of separating interlinked DNA molecules, such as sister chromatids or circular genomes, by breaking and rejoining strands.
References
- Elucidation of an essential function of the unique charged domain of Plasmodium topoisomerase III.. Biochemical Journal (2020).
- Nonintercalative antitumor drugs interfere with the breakage-reunion reaction of mammalian DNA topoisomerase II.. Journal of Biological Chemistry (1984).
- Purification of a DNA topoisomerase II from the hyperthermophilic archaeon Sulfolobus shibatae. A thermostable enzyme with both bacterial and eucaryal features.. Journal of Biological Chemistry (1994).
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