{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nDNA polymerase beta (POLB) is a central enzyme in the base excision repair (BER) pathway, where it functions chiefly as the gap‐filling polymerase in both single‐nucleotide and long‐patch BER. In multiple studies its activity has been linked to proper processing of simple base lesions, single‐strand breaks, and abasic sites, and its timely recruitment—often via transient complexes with repair proteins such as XRCC1, FEN1, and ligase complexes—is critical for maintaining genomic stability. POLB expression and genetic variability have been examined in the context of cancer risk and DNA damage resistance, and these investigations underscore its pivotal role in repair as well as its regulation by protein–protein interactions and ubiquitylation pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nHigh-resolution structural and mechanistic studies have revealed how POLB achieves catalytic efficiency and fidelity. Crystallographic analyses have demonstrated that dynamic adjustments at its active site—including transient metal ion binding and specific interactions with the nucleoside triphosphate—promote correct nucleotide insertion while deterring misincorporation, especially during repair of oxidative lesions such as 8-oxodG. Such investigations have dissected important features ranging from ribonucleotide discrimination by active-site residues (for example, Lys-280 and Tyr-271) to differences in conformational commitment during substrate binding and catalysis. These insights provide a molecular basis for understanding POLB’s contribution to polymerase fidelity and overall genome integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical repair function, dysregulation and cancer-associated variants of POLB have been implicated in tumorigenesis and genomic instability. Several studies have identified germline and somatic mutations—such as the P242R and L22P variants—that compromise its polymerase and dRP lyase activities, alter its interactions with partners like PCNA, p300, and XRCC1, and lead to the accumulation of improper repair intermediates. In some experimental models, overexpression of the error-prone POLB has been shown to perturb replication fidelity, promote aneuploidy, and shift repair pathway utilization, thereby contributing to a mutator phenotype that may drive cancer progression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Shanbeh Zienolddiny, Daniele Campa, Helge Lind, et al. 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