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.
Todorova
Roumiana
R
Institute of Biophysics, Bulgarian Academy of Sciences, Acad. Georgi Bonchev str., Bl. 21, 1113, Sofia, Bulgaria. todorova@obzor.bio21.bas.bg
D001665:Binding Sites; D015153:Blotting, Western; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D011485:Protein Binding; D012319:RNA Polymerase II / Q000378:metabolism*; D034802:RNA-Binding Protein EWS / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
D034802:RNA-Binding Protein EWS; C477608:POLR2G protein, human; D012319:RNA Polymerase II