文摘
NFAT transcription factors play a central role in initiating T-cell activation through the inductionof immediate-early T-cell specific genes including interleukin-2 (IL-2). NFAT transcription factors bindto a sequence in the IL-2 enhancer known as the antigen receptor response element 2 (ARRE-2). Multipleproteins exhibiting ARRE-2 binding activity have been isolated, including a heterodimer from stimulatedT-cell nuclear extracts consisting of Mr = 90 000 (NF90) and Mr = 45 000 (NF45) subunits. The subunitsof this heterodimer have been cloned, and NF90 was found to encode a protein containing two domainsthat are predicted to form motifs capable of binding to double-stranded RNA. Using in vitro translatedpolypeptides, we have demonstrated that NF90 specifically binds to double-stranded RNA. Furthermore,NF90 was phosphorylated in a double-stranded RNA-dependent manner likely by the interferon-induced,double-stranded RNA-dependent protein kinase, PKR. The NF90 protein was found to be expressed notonly in T-cells, but also in nonimmune HeLa cells. In HeLa cells, the protein was almost exclusivelylocalized to the ribosome salt wash fraction of cell lysates.