background:
DNA replication, recombination and repair, all of which are necessary for genomic stability, require the presence of exonucleases (1). In DNA replication, these enzymes are involved in the processing of Okazaki fragments, whereas in DNA repair, they function to excise damaged DNA fragments and correct recombinational mismatches (2). These exonucleases include the family of DNA polymerases (3). DNA pol α, β, ∂, and e are involved in DNA replication and repair (4). DNA pol ∂ and DNA pol e are multisubunit enzymes, with DNA pol ∂ consisting of two subunits p125, which interacts with the sliding DNA clamp protein PCNA, and p50 (5). The nuclear-encoded DNA pol © is the only DNA polymerase required for the replication of the mitochondrial DNA (6). DNA pol Ω is ubiquitously expressed in various tissues and mediates the cellular mechanism of damage-induced mutagenesis (7). DNA pol œ is a DNA polymerase-helicase that binds ATP and is involved in the repair of interstrand crosslinks (8).
Function:
Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.
Subcellular Location:
Monomer. Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47.
Post-translational modifications:
Methylation by PRMT6 stimulates the polymerase activity by enhancing DNA binding and processivity.
Similarity:
Belongs to the DNA polymerase type-X family.
Database links:
UniProtKB/Swiss-Prot: Q15653.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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