
Binding of eIF4G1 and eIF4G1 fragments to poly(U) agarose. Purified GST-eIF4G1 fusion proteins were bound to poly(U) agarose for 30 min at 4°C, the resin washed extensively with buffer, proteins bound to the matrix eluted by boiling with SDS sample buffer, fractionated on 17.5% SDS polyacrylamide gels, and stained with Coomassie blue. Where indicated, the protein was preincubated for 15 min with soluble poly(U). For each fusion protein, unbound protein (NB) and protein bound to the matrix (B) in the absence (first and second lanes) and in the presence (third and fourth lanes) of soluble poly(U) is shown.










