Flap endonuclease-1 (FEN-1) is a structure-specific nuclease with multiple functions in DNA processing pathways. The replication and DNA repair activities of FEN-1 are critical for genomic stability in the eukaryotic cell. Through interaction with proliferation cell nuclear antigen (PCNA), FEN-1 helps coordinate Okazaki fragment maturation by removing RNA-DNA primers. FEN-1 is also required for non-homologous end joining of double stranded DNA breaks in long patch base excision repair. The multi-functional activities of FEN-1 are regulated by various mechanisms, including protein partner interactions, post-translational modifications, and subcellular re-localization in response to cell cycle or DNA damage.
Flap endonuclease-1 (FEN-1) is a structure-specific nuclease with multiple functions in DNA processing pathways. The replication and DNA repair activities of FEN-1 are critical for genomic stability in the eukaryotic cell. Through interaction with proliferation cell nuclear antigen (PCNA), FEN-1 helps coordinate Okazaki fragment maturation by removing RNA-DNA primers. FEN-1 is also required for non-homologous end joining of double stranded DNA breaks in long patch base excision repair. The multi-functional activities of FEN-1 are regulated by various mechanisms, including protein partner interactions, post-translational modifications, and subcellular re-localization in response to cell cycle or DNA damage.
This protein removes 5 overhanging flaps in DNA repair and processes the 5 ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5 end of the flap that is necessary for both binding and cleavage by This protein. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions., This protein removes 5 overhanging flaps in DNA repair and processes the 5 ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5 end of the flap that is necessary for both binding and cleavage by This protein. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA., Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Pathway
DNA repair pathway, DNA repair pathway
Protein Families
XPG/RAD2 endonuclease family, FEN1 subfamily
Buffer
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3., Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Format
liquid
Purification
Affinity purification
Purity
Affinity purification
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Storage Buffer
Store at -20oC or -80oC. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.