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DNA primase large subunit (PRIM2, also known as p58) is an enzyme that forms a heterodimer with a smaller primase subunit (p49), together constituting the primase component of the DNA polymerase alpha-primase complex in eukaryotes[1][4][6]. This complex is essential for chromosomal DNA replication, as it synthesizes short RNA primers that are extended by DNA polymerases to form Okazaki fragments on the lagging strand and initiate leading strand synthesis[1][7]. The 58 kDa large subunit is encoded by the PRIM2 gene in humans and acts as a regulatory and structural partner to the catalytic small subunit during primer formation[1][6][7]. While PRIM2 is fundamental for cell proliferation, there are currently no reported small-molecule drugs or approved inhibitors that specifically target this enzyme in clinical use, and no established biomarker or mechanism-of-action drugs identified from current search results[6][7]. Impairment of PRIM2 function is expected to disrupt DNA replication, which can result in cell cycle arrest or cell death.
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