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A Closer Look at the 5′-End of mRNA in Relation to Initiation

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Part of the book series: NATO Advanced Study Institutes Series ((NSSA,volume 41))

Abstract

Eukaryotic mRNAs are generally monocistronic (1, 2). Ribosomes attach at or near the 5′-end of the mRNA, and translation is limited to the 5′-proximal cistron (3, see preceding chapter of this volume). By contrast, on prokaryotes ribosomes initiate protein synthesis on some mRNAs at multiple internal sites, resulting in polycistronic translation (4). Two kinds of mRNA structural features may account at least in part for this functional difference between the messages of higher and lower organisms. One is the 5′-terminal cap structure, m7G (5′)ppp(5′)N, which is unique to eukaryotic cellular and most viral mRNAs (5). A variety of experimental findings indicate that the presence of a cap promotes translation by facilitating stable binding of ribosomes (6, 7). Implied from these results is a recognition of the cap by putative cap binding proteins during initiation of protein synthesis. Messengers in bacteria apparently are not methylated or otherwise modified and nascent transcripts are read directly by a process of coupled transcription/translation (8). The mRNAs of prokaryotes include a purine-rich sequence, located ~10 nucleotide upstream from initiator triplets, that helps to stabilize initiation complexes by base-pairing with the 3′-terminal end of 16S ribosomal RNA (4, 9).

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Shatkin, A.J. (1982). A Closer Look at the 5′-End of mRNA in Relation to Initiation. 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_8

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  • DOI: https://doi.org/10.1007/978-1-4684-4124-6_8

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