ATP-dependent DNA helicase PIF1 (PIF1)

ATP-dependent DNA helicase PIF1 (PIF1) is a highly conserved, multifunctional enzyme involved in unwinding DNA in the 5'-to-3' direction[2][3]. It plays crucial roles in the maintenance of nuclear and mitochondrial DNA integrity in eukaryotes, facilitating replication fork progression through barriers like G-quadruplexes and protein blocks, thus reducing genetic instability at these sites[2][4][1]. In yeast, Pif1 negatively regulates telomerase and participates in Okazaki fragment processing and break-induced DNA repair[2][4]. In humans, PIF1 supports unperturbed genome-wide replication fork progression and helps prevent genome instability by unwinding secondary DNA structures that stall replication[1]. Structurally, PIF1 belongs to superfamily 1B helicases, containing a conserved core helicase domain with accessory regions for protein interactions. Mutations such as L319P can abolish helicase function and are linked to cancer risk[2]. No approved drugs currently target PIF1 directly; however, its critical functions in genome maintenance make it a potential therapeutic target for conditions involving replication stress, DNA repair defects, or telomerase activity regulation[1][2][3][4][5].

Other names

PIF1C15orf20FLJ22692DNA 5'-3' helicase PIF1DNA repair and recombination helicase PIF1PIF1/RRM3 DNA helicase-like proteinPIFpetite integration frequency 1