作者: T. W. REICHMAN
DOI: 10.1261/RNA.2181103
关键词:
摘要: Nuclear factor 110 (NF110) belongs to the nuclear 90 (NF90) family of double-stranded RNA (dsRNA) binding proteins that regulate gene expression at transcriptional level in vertebrates. The are identical their N terminus, which functions as a negative regulatory region, but have distinct C termini result alternate splicing. Maximal activity NF110 requires its C-terminal domain and central contains localization signal two dsRNA-binding motifs (dsRBMs). We find dsRNA is reduced by RGG GQSY present region. To directly evaluate role transactivation, we conducted site-directed mutagenesis substitute conserved residues one or both dsRBMs. mutations ability stimulate an extent paralleled mutants’ bind dsRNA. Full was restored when dsRBM-containing region replaced with RNA-binding protein kinase PKR. Finally, NF110-mediated transactivation inhibited cotransfection plasmid encoding artificial highly structured RNA. These data suggest homologs regulated cis-acting domains some isoforms, via interactions RNAs propose model modulating transcription through members NF90 family.