Akabayov, Sabine R.Akabayov, BarakWagner, Gerhard2015-10-012014Akabayov, Sabine R., Barak Akabayov, and Gerhard Wagner. 2014. “Human Translation Initiation Factor eIF4G1 Possesses a Low-Affinity ATP Binding Site Facing the ATP-Binding Cleft of eIF4A in the eIF4G/eIF4A Complex.” Biochemistry 53 (41): 6422-6425. doi:10.1021/bi500600m. http://dx.doi.org/10.1021/bi500600m.0006-2960http://nrs.harvard.edu/urn-3:HUL.InstRepos:22856978Eukaryotic translation initiation factor 4G (eIF4G) plays a crucial role in translation initiation, serving as a scaffolding protein binding several other initiation factors, other proteins, and RNA. Binding of eIF4G to the ATP-dependent RNA helicase eukaryotic translation initiation factor 4A (eIF4A) enhances the activity of eIF4A in solution and in crowded environments. 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 enhancement in activity.en-USAccelerated PublicationJournal Article2015-10-0110.1021/bi500600m