DNA primase and DNA ligase

DNA primase and DNA ligase are two distinct classes of enzymes essential for the maintenance and replication of the genome (PubMed 27535915). DNA primase, typically functioning within the DNA polymerase alpha-primase complex, is responsible for synthesizing short RNA primers that provide the essential 3'-OH group required for DNA polymerases to initiate synthesis, particularly on the lagging strand (UniProt P49642). DNA ligase subsequently seals the nicks between DNA fragments, such as Okazaki fragments, by catalyzing the formation of phosphodiester bonds between the 3'-hydroxyl and 5'-phosphate ends (UniProt P18858). While both are critical components of the replisome and are investigated as therapeutic targets in oncology and infectious diseases, they are separate proteins with unique catalytic mechanisms (PubMed 30249624). Inhibiting these enzymes leads to stalled replication forks, DNA double-strand breaks, and ultimately cell death, making them attractive for targeting rapidly dividing cancer cells or pathogens (PubMed 28910176). This target entry is considered incorrect as it conflates two distinct enzyme families that, while functionally related in the DNA replication pathway, are encoded by different genes and possess different active sites.

Other names

DNA primaseDNA ligaseDNA replication machineryReplisome components

Inhibition of RNA primer synthesis (primase) and DNA strand ligation (ligase) to disrupt DNA replication and repair.