Abstract
We have previously shown that a GTP derivative bearing p-azidoaniline at the γ-phosphate group specifically labels the γ-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 β-subunit of eIF-2 was found to be specifically labeled in all complexes investigated. It is concluded that GTP interacts with both the β- and γ-subunit of eIF-2: the guanosine moiety is in contact with the β-subunit and the γ-phosphate group with the γ-subunit.
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