Zinc finger GRF-type containing 1 (ZGRF1)

Zinc finger GRF-type containing 1 (ZGRF1) is a nuclear DNA repair enzyme that contains a GRF-type zinc finger domain and a transmembrane region. It functions as a 5'-3' DNA helicase, crucial for resolving replication-blocking DNA lesions via homologous recombination. ZGRF1 physically interacts with the recombinase RAD51, stimulating strand exchange and promoting DNA repair. It catalyzes D-loop dissociation and Holliday junction branch migration, thereby ensuring genome stability. Loss of ZGRF1 impairs the repair of double-strand breaks, leads to chromosome aberrations, and hypersensitizes cells to agents inducing replication stress. Genetic variation within ZGRF1 has been implicated, albeit poorly understood, in metabolic phenotypes such as central fat deposition. The protein exhibits relatively low basal expression with cell cycle-regulated upregulation, notably peaking in S phase. Although not a direct target of drugs, ZGRF1 is vital for the cellular response to genotoxic chemotherapies by maintaining DNA integrity and preventing genome instability[1][2][3][4].

Other names

ZGRF1C4orf215'-3' DNA helicase ZGRF1GRF-type zinc finger domain-containing protein 1FLJ11331protein ZGRF1

Drugs causing DNA crosslinks or replication stress (e.g., mitomycin C, camptothecin) engage ZGRF1-mediated repair pathways, but ZGRF1 is not a direct pharmacological target[4].