{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nDNA polymerase λ (pol λ or POLL) is a multifunctional, Family X polymerase that is integral to maintaining genome stability by participating in several DNA repair pathways. It fills short gaps during base excision repair as well as nonhomologous end joining (NHEJ) of DNA double‐strand breaks, performing template–dependent nucleotide incorporation, terminal transferase, and deoxyribose phosphate lyase activities. POLL’s gap‐filling ability is especially important for restoring DNA integrity after oxidative damage, abasic site formation, and free radical–mediated strand breaks, and it is capable of extending mismatched primer termini and engaging in translesion synthesis to bypass lesions such as 8‑oxo‑guanine and 2‑oxo‑adenine."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDetailed pre–steady state kinetic and crystallographic studies have revealed that POLL achieves high nucleotide affinity and selective incorporation through cooperative interactions between conserved active‐site residues and its substrates. Its unique domain structure—including a BRCT domain and regulatory regions—enables local conformational adjustments (such as template “scrunching”) that optimize gap‐filling and mismatch extension, while its active site discriminates against improper nucleotides to ensure repair fidelity. These mechanistic insights explain POLL’s ability to extend from mispaired ends and process diverse DNA structures encountered during repair."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its catalytic core, POLL is tightly regulated by interactions with accessory proteins—such as PCNA, XRCC4, and various DNA repair factors—and through post–translational modifications like phosphorylation and ubiquitination. These regulatory inputs govern its recruitment to DNA damage sites and modulate its activity during the cell cycle, ensuring timely and accurate repair even in the presence of bulky adducts or misincorporated ribonucleotides. This multifaceted control is critical for preventing mutagenesis and suppressing genome instability under stress conditions, thereby impacting cancer development and cellular responses to genotoxic agents."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Miguel García-Díaz, Katarzyna Bebenek, Rosario Sabariegos, et al. 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