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

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 . (Access to this publication is restricted)

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http://dx.doi.org/10.1073/pnas.0606880104

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.

Item Type: Article
Uncontrolled keywords: posttranscriptional gene expression; protein synthesis; ribosome structure
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Tobias von der Haar
Date Deposited: 08 Jul 2008 13:32
Last Modified: 15 Jul 2014 08:50
Resource URI: http://kar.kent.ac.uk/id/eprint/5336 (The current URI for this page, for reference purposes)
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