Swi5-dependent homologous recombination repair protein 1 (SFR1)

Swi5-dependent homologous recombination repair protein 1 (SFR1) is a key auxiliary factor partnering with SWI5 and functioning in the repair of DNA double-strand breaks via homologous recombination[1][3][5]. SFR1 forms a heterodimeric complex with Swi5, which physically interacts with and stabilizes the RAD51 recombinase filament, enhancing DNA strand exchange and maintaining the active ATP-bound state of the filament[3][5]. SFR1’s function is regulated by cyclin-dependent kinase (CDK)-mediated phosphorylation, which modulates its affinity for RAD51 and consequently controls homologous chromosome recombination during meiosis[2][4]. Loss or mutation of SFR1 or its complex partner Swi5 results in impaired DNA repair, genomic instability, and sensitivity to DNA-damaging agents such as ionizing radiation, camptothecin, and PARP inhibitors like olaparib[1][5]. Although crucial for genome integrity, SFR1 is not considered a primary therapeutic target and is not directly targeted by existing drugs[1][5].

Other names

Swi5-dependent recombination DNA repair protein 1 homologSFR1C10orf78MEI5MEIR5bA373N18.1FLJ41960Meiosis protein 5 homolog

DNA repair pathway augmentation (influences cellular response to DNA damaging agents via homologous recombination regulation); not a direct drug target