Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex

John Mccarthy, Robert J C Gilbert, Yulya Gordiyenko, Tobias Von Der Haar, Andreas F P Sonnen, Gregor Hofmann, Maria Nardelli, David I. Stuart, John E G McCarthy

    Research output: Contribution to journalArticlepeer-review

    Abstract

    In the process of protein synthesis, the small (40S) subunit of the eukaryotic ribosome is recruited to the capped 5′ end of the mRNA, from which point it scans along the 5′ untranslated region in search of a start codon. However, the 40S subunit alone is not capable of functional association with cellular mRNA species; it has to be prepared for the recruitment and scanning steps by interactions with a group of eukaryotic initiation factors (eIFs). In budding yeast, an important subset of these factors (1, 2, 3, and 5) can form a multifactor complex (MFC). Here, we describe cryo-EM reconstructions of the 40S subunit, of the MFC, and of 40S complexes with MFC factors plus eIF1A. These studies reveal the positioning of the core MFC on the 40S subunit, and show how eIF-binding induces mobility in the head and platform and reconfigures the head-platform-body relationship. This is expected to increase the accessibility of the mRNA channel, thus enabling the 40S subunit to convert to a recruitment-competent state. © 2007 by The National Academy of Sciences of the USA.
    Original languageEnglish
    Pages (from-to)5788-5793
    Number of pages5
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume104
    Issue number14
    DOIs
    Publication statusPublished - 3 Apr 2007

    Keywords

    • Posttranscriptional gene expression
    • Protein synthesis
    • Ribosome structure

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