Human FUS, C-His Tag Protein

EWS and FUS/TLS are nuclear RNA-binding proteins. As a result of chromosome translocation, the EWS gene is fused to a variety of transcription factors, including ATF-1, in human neoplasias. In the Ewing family of tumors, the N-terminal domain of EWS is fused to the DNA-binding domain of various Ets transcription factors, including Fli-1, ETV1 and FEV. The EWS/Fli-1 chimeric protein acts as a more potent transcriptional activator than Fli-1 and can promote cell transformation. In human myxoid liposarcomas and myeloid leukemias, chromosomal translocation results in the fusion of the N-terminal region of FUS/TLS with the open reading frame of CHOP. In normal cells, FUS/TLS binds to the DNA-binding domains of nuclear steroid receptors and is also present in subpopulations of TFIID complexes, indicating a potential role for FUS/TLS in the processing of primary transcripts that are generated in response to hormone-induced transcription.