Though a shared feature of DNA ligases is their envelopment with the nicked duplex like a C-formed protein clamp, they carry out this feat by using remarkably unique accessory structural modules and domain topologies. As structural, biochemical, and phylogenetic insights coalesce, we can easily hope advances on numerous fronts, which include (i) pharmacological targeting of ligases for antibacterial and anticancer therapies and (ii) the discovery and design of new strand-sealing enzymes with exclusive substrate specificities.

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NAD+-dependent DNA ligases (generally known as LigA) are a distinctive and structurally homogeneous clade of enzymes present in all microbes. Escherichia coli

An engineered action 3 arrest mutant of DNA ligase would, if widely Lively, pepper the genome with unresected 5′-adenylates at sites of DNA repair or joining of Okazaki fragments. This may be catastrophic if the level of DNA five′-adenylylation exceeds the cell's capacity to get rid of the lesions (33). Such a state of affairs is analogous to “poisoning” of topoisomerase IB by camptothecin medicine or drug-mimetic enzyme mutations that selectively impede the DNA ligation action from the topoisomerase pathway.

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