Abstract
FOR some time guanosine triphosphate (GTP) has been known to be involved in the initiation of bacterial protein synthesis1–4, although its exact function remains obscure. Although GTP stimulates the binding of fMet-tRNA to 30S ribosomes5,6, it does not seem to be hydrolysed in the process7. Hydrolysis is thought to occur later, either during or immediately after the junction of the 30S initiation complex (composed of a 30S ribosome, fMet-tRNA, mRNA, initiation factor F1, and probably other components as we shall show; and hereafter referred to as 30S i-complex) with a 50S ribosome to form a 70S initiation complex7–9. The use to which the energy released in this hydrolysis step is put is not yet known for certain.
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