Bacterial DNA primase (DnaG)

Bacterial DNA primase, primarily known as DnaG, is an essential enzyme within the bacterial replisome responsible for synthesizing short RNA primers (NIH, 2018; Wikipedia). These primers are critical for the initiation of DNA synthesis by DNA polymerase, particularly on the lagging strand where they initiate the formation of Okazaki fragments (NIH, 2015; Wikipedia). Because DNA polymerases cannot start DNA synthesis de novo, the activity of primase is indispensable for bacterial cell division and survival (ASM, 2017; Wikipedia). Structurally, bacterial primases are distinct from their eukaryotic counterparts, typically consisting of three domains: a zinc-binding domain for DNA recognition, an RNA polymerase domain for catalysis, and a helicase-binding domain for interaction with the DnaB helicase (NIH, 2018; ResearchGate). This structural divergence makes bacterial DNA primase an attractive target for the development of novel antibiotics, especially against drug-resistant pathogens like Mycobacterium tuberculosis (IJARBS, 2023; ASM, 2017). Inhibitors of this enzyme, such as certain small molecules and natural products, work by halting the replication fork, which ultimately leads to bacteriocidal effects (NIH, 2018; ResearchGate).

Other names

DnaGDnaG primasednaPDNA-dependent RNA polymerase

Inhibition of RNA primer synthesis, halting DNA replication.