Human translation initiation factor eIF4G1 possesses a low-affinity ATP binding site facing the ATP-binding cleft of eIF4A in the eIF4G/eIF4A complex. Academic Article uri icon

abstract

  • The eukaryotic translation initiation factor eIF4G plays a crucial role in translation initiation serving as a scaffolding protein binding several other initiation factors, other proteins as well as RNA. Binding of eIF4G to the ATP-dependent RNA helicase eIF4A enhances the activity of eIF4A in solution and in crowded environment. Previously, this activity enhancement was solely attributed to eIF4G conferring a closed/active conformation upon eIF4A. Here we show that eIF4G contains a low-affinity binding site at the entrance to the ATP-binding cleft on eIF4A suggesting that regulation of the local ATP concentration may be an additional reason for the activity enhancement.

publication date

  • October 1, 2014