In vitro interaction between the N-terminus of the Ewing's sarcoma protein and the subunit of RNA polymerase II hsRPB7.

In vivo and in vitro expressed N-terminal sequence of EWS (EAD) and hsRPB7 (subunit of human RNA polymerase II) were probed for protein-protein interactions using pull-down assays. In result, it was found that the proteins 57Z (residues 1-57 of EAD) and hsRPB7 interact in vitro forming a stable complex. The direct interaction between 57z and hsRPB7 indicate that DHR-related peptides and other small molecules, targeted to N-terminus of EWS might possess therapeutic potentialities as anti-cancer agents to function as inhibitors of EAD-mediated transactivation.