Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (   ). Required for double-strand break repair and V(D)J recombination (   ). Also has a role in chromosome translocation (   ). Has a role in chromosome translocation (   ). The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner (   ). It works in the 3'-5' direction (   ). During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection (   ). Binding to DNA may be mediated by XRCC6 (   ). The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold (   ). The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together (   ). The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step (   ). Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks . 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined . The XRCC5-XRRC6 dimer together with APEX1 acts as a negative regulator of transcription . In association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin promoter and activates osteocalcin expression . Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway .
Subcellular locations: Nucleus, Chromosome