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The translation initiation factor eIF4G is required for the translation of many eukaryotic messenger RNAs. Its interaction with the ATP-dependent RNA helicase eIF4A plays an important role in the regulation of translation initiation. eIF4G in humans and other higher eukaryotes contains three HEAT domains, of which HEAT1 and HEAT2 contain binding sites for eIF4A. Here we report the near complete NMR resonance assignment of the 192-residue HEAT2 domain of the human translation initiation factor eIF4GI. The chemical shift data constitute the basis for NMR structural studies aimed at expanding understanding of the role of interactions between the initiation factor eIF4A and eIF4G in translation initiation.

1H, 13C, and 15N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI