[HTML][HTML] EWS· Fli-1 fusion protein interacts with hyperphosphorylated RNA polymerase II and interferes with serine-arginine protein-mediated RNA splicing
L Yang, HA Chansky, DD Hickstein - Journal of Biological Chemistry, 2000 - ASBMB
Ewing's sarcoma displays a characteristic chromosomal translocation that results in fusion of
the N-terminal domain of the Ewing's sarcoma protein (EWS) to the C-terminal DNA-binding
domain of the ETS family transcription factor Fli-1 (Friend leukemia integration-1). EWS
possesses structural motifs suggesting a role in transactivation as well as RNA binding. We
demonstrate that wild-type EWS protein functions as an adapter molecule coupling
transcription to RNA splicing by binding to hyperphosphorylated RNA polymerase II through …
the N-terminal domain of the Ewing's sarcoma protein (EWS) to the C-terminal DNA-binding
domain of the ETS family transcription factor Fli-1 (Friend leukemia integration-1). EWS
possesses structural motifs suggesting a role in transactivation as well as RNA binding. We
demonstrate that wild-type EWS protein functions as an adapter molecule coupling
transcription to RNA splicing by binding to hyperphosphorylated RNA polymerase II through …