Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).

摘要: Various Sarcophaga peregrina (flesh fly) defense protein genes were shown to be activated when NIH-Sape-4 cells cultured with bacterial lipopolysaccharides or beta-1,3-glucan. The 5' upstream regions of the found have common motifs showing similarity mammalian NF-kappa B-binding consensus sequence. A affinity motif lectin promoter was identified and purified near homogeneity. This 59-kDa also bound other genes, e.g., sarcotoxin I II genes. in both cytoplasmic nuclear fractions cells, it appeared migrate from cytoplasm nucleus on treatment lipopolysaccharides. is probably a transcriptional regulator for proteins S. peregrina.