GTP interacts through its ribose and phosphate moieties with different subunits of the eukaryotic initiation factor eIF‐2

This is the authors' abstract. We don't add key points for this paper.

We have previously shown that a GTP derivative bearing p-azidoaniline at the gamma-phosphate group specifically labels the gamma-subunit of eukaryotic initiation factor eIF-2. In the present study a new GTP derivative carrying the photoreactive group at the ribose moiety of GTP was applied for affinity labeling of eIF-2 in different initiation complexes. Using this GTP analogue the beta-subunit of eIF-2 was found to be specifically labeled in all complexes investigated. It is concluded that GTP interacts with both the beta- and gamma-subunit of eIF-2: the guanosine moiety is in contact with the beta-subunit and the gamma-phosphate group with the gamma-subunit.