Abstract
The step of protein synthesis which is normally rate limiting, formation of the 48S initiation complex, is catalyzed by the group 4 initiation factors. Collectively they recognize the 7-methylguanosine-containing cap of mRNA, unwind mRNA secondary structure, and allow scanning for the initiation codon by the small ribosomal subunit. The activities of the elF-4 polypeptides are modulated by phosphorylation. Recent studies shed new light on the mechanism of assembly of the 48S initiation complex and the effect of phosphorylation of one of the elF-4 polypeptides, the cap-binding protein elF-4E.
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