eIF5B plays an important role in later stages of the translation initiationmechanism. After the start codon has been engaged by the scanning initiation complex, eukaryotic initiation factorseIF1, eIF2, and eIF5leave the ribosome. Subsequently, eIF5B-GTP is recruited to the ribosome. eIF1Ainduces rotation of a domain of eIF5B-GTP, which in turn positions the initiator tRNA such that joining of the large ribosomal subunit is possible. Joining of the large subunitcauseshydrolysis of the eIF5B-bound GTP, which accelerates the release of eIF1A from the ribosome. Dissociation of eIF1A leads to another rearrangement of eIF5B, placing the initiator tRNA in its final position. The hydrolysis of eIF5B's GTP reduces its affinity to the ribosome, ultimately leading to its dissociation. This concludes the initiation of translation.