Novel insights into the architecture and protein interaction network of yeast eIF3

Mapping the interaction network of eIF3 by analytical SEC. (A) Full-length Prt1 interacts with the C-terminal region of Tif32. This interaction is not visible when the full-length Prt1 is replaced with a fragment starting from residue 181 (Prt1^181C). (B) Nip1 interacts with Prt1-Tif34-Tif35 complex but not with each protein individually. Vertical lines are drawn to facilitate the comparison of the retention volumes of Nip1, Prt1, or Prt1^181C in different experiments. In each case, the thick bar at the bottom of the graphs represents the fractions of the peak, which is resolved by SDS-PAGE.