The initiation of mammalian protein synthesis and the mechanism of scanning

By I. Lomakin, T. Steitz. 2013

110 citations recorded by the source corpus.

During translation initiation in eukaryotes, the small ribosomal subunit binds messenger RNA at the 5′ end and scans in the 5′ to 3′ direction to locate the initiation codon, form the 80S initiation complex and start protein synthesis. This simple, yet intricate, process is guided by multiple initiation factors. Here we determine the structures of three complexes of the small ribosomal subunit that represent distinct steps in mammalian translation initiation. These structures reveal the locations of eIF1, eIF1A, mRNA and initiator transfer RNA bound to the small ribosomal subunit and provide insights into the details of translation initiation specific to eukaryotes. Conformational changes associated with the captured functional states reveal the dynamics of the interactions in the P site of the ribosome. These results have functional implications for the mechanism of mRNA scanning.

Subfields: Molecular Biology

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In Molecular Biology

1. M. Sokabe
2. Y. Hashem
3. C. Fraser
4. A. Hinnebusch

Citations in the corpus

• Structural Insights into the Mammalian Late-Stage Initiation Complexes (2020, background): “With few exceptions, this eIF1A NTT is highly conserved among eukaryotes (Figure 2D).”
• Toward a Kinetic Understanding of Eukaryotic Translation. (2018, background): “However, other initiation components may contribute to stabilizing this conformation because structures of 40S subunit complexes that include eIF1 and eIF1A adopt a closed conformation (Hashem et al. 2013; Lomakin and Steitz 2013; Weisser et al. 2013).”