DNA polymerase lambda (Pol λ)

DNA polymerase lambda is a eukaryotic DNA repair enzyme, encoded by the POLL gene in humans, and a member of the X family of DNA polymerases[1][3]. It is primarily involved in DNA double-strand break repair by non-homologous end joining and in base excision repair, functioning mainly to fill short gaps during these processes[1][3][5]. Structurally, it possesses a catalytic polymerase domain, an 8 kDa lyase domain (removing 5′-deoxyribose phosphate), and a BRCT domain for protein interactions, enabling it to stabilize DNA ends and bridge gaps[1][3]. DNA polymerase lambda is also implicated in certain translesion DNA synthesis events and contributes to immune system diversity via V(D)J recombination. Its fidelity differs from replicative polymerases, with an error profile marked by relatively high rates of single-nucleotide deletions[3]. While no approved therapeutics directly target Pol λ, its central role in repair pathways positions it as a potential research target in oncology and immunology[1][3][5].

Other names

POLLDNA polymerase lambda (human gene symbol: POLL)Pol lambda

Not applicable; no specific drugs target Pol λ directly. Its inhibition or modulation would, in principle, impair DNA double-strand break repair via NHEJ/BER and potentially sensitize cells to DNA damage.