Eukaryote polypeptide chain initiation factor (eIF4G) binds with the mRNA cap-binding protein eIF4E and the ATP-dependent RNA helicase eIF4A, which constitute the translation initiation factor eIF4F complex. eIF4G plays an important role in the mechanism of translation by binding with other components of the ribosomal initiation factors. Two forms of eIF4G have been reported as two different gene products eIF4G1 and eIF4G2. eIF4G1 is a single polypeptide chain of approximately 154 kDa. The association of eIF4E with eIF4G1 results in the formation of a protease-resistant, 98-residue fragment of eIF4G1. NMR analysis revealed that this residue unfolds in the absence of eIF4E and is almost completely folded in the presence of eIF4E. It is suggested that binding with eIF4E creates a new binding surface on eIF4G1 that allows for the binding of other factors of the translational machinery. It has been suggested that interaction of PABP with eIF4G1 facilitates the functional association of the 3’ end of an mRNA with the 5’ end.