Abstract
The mechanism by which ribosomes select the correct AUG codon for initiation of protein synthesis has been the subject of considerable speculation and experimentation. In the case of prokaryotic messages and ribosomes, there is convincing evidence supporting Shine and Dalgarno’s proposal (1) that base pairing occurs between the pyrimidine-rich 3′-end of 16S ribosomal RNA and a purine-rich sequence located approximately 10 nucleotides to the left of the AUG or GUG initiator codon (2–4). This interaction plays a central role in recognition of initiation sites by E. coli ribosomes, although additional features in the message also influence the efficiency of ribosome binding (5–8). Eukaryotic translational systems display certain peculiarities which argue against the notion that the mechanism of initiation in eukaryotes is more-or-less an extension of the accepted prokaryotic mechanism. For example, the monocistronic character of eukaryotic messenger RNAs (9–11) and the facilitating effect of the 5′-terminal m7G cap (12) are features, not observed in prokaryotes, which must be assimilated into any model for translational initiation in eukaryotes.
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© 1982 Plenum Press, New York
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Kozak, M. (1982). Recognition of Initiation Sites in Eukaryotic Messenger RNAs. In: Pérez-Bercoff, R. (eds) Protein Biosynthesis in Eukaryotes. NATO Advanced Study Institutes Series, vol 41. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4124-6_7
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