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The initiation of mammalian protein synthesis and mRNA scanning mechanism

Author

Listed:
  • Ivan B. Lomakin

    (Yale University)

  • Thomas A. Steitz

    (Yale University
    Howard Hughes Medical Institute, Yale University)

Abstract

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.

Suggested Citation

  • Ivan B. Lomakin & Thomas A. Steitz, 2013. "The initiation of mammalian protein synthesis and mRNA scanning mechanism," Nature, Nature, vol. 500(7462), pages 307-311, August.
    • Handle: RePEc:nat:nature:v:500:y:2013:i:7462:d:10.1038_nature12355
    DOI: 10.1038/nature12355
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    Cited by:

    1. Anna B. Loveland & Egor Svidritskiy & Denis Susorov & Soojin Lee & Alexander Park & Sarah Zvornicanin & Gabriel Demo & Fen-Biao Gao & Andrei A. Korostelev, 2022. "Ribosome inhibition by C9ORF72-ALS/FTD-associated poly-PR and poly-GR proteins revealed by cryo-EM," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Runlai Hang & Hao Li & Wenjing Liu & Runyu Wang & Hao Hu & Meng Chen & Chenjiang You & Xuemei Chen, 2024. "HOT3/eIF5B1 confers Kozak motif-dependent translational control of photosynthesis-associated nuclear genes for chloroplast biogenesis," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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