Gilbert, Robert J.C. and Gordiyenko, Yulya and von der Haar, Tobias and Sonnen, Andreas F.P. and Hofmann, Gregor and Nardelli, Maria and Stuart, David I. and McCarthy, John E. G. (2007) Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex. Proceedings of the National Academy of Sciences of the United States of America, 104 (14). pp. 5788-5793. ISSN 0027-8424 . (doi:https://doi.org/10.1073/pnas.0606880104 ) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided)
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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.
|Uncontrolled keywords:||posttranscriptional gene expression; protein synthesis; ribosome structure|
|Divisions:||Faculties > Sciences > School of Biosciences > Protein Science Group|
|Depositing User:||Tobias von der Haar|
|Date Deposited:||08 Jul 2008 13:32 UTC|
|Last Modified:||15 Jul 2014 08:50 UTC|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/5336 (The current URI for this page, for reference purposes)|