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-Structure paper
Title | Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 104, Issue 14, Page 5788-5793, Year 2007 |
Publish date | Apr 3, 2007 |
Authors | 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 / |
PubMed 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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:17389391 / PubMed Central |
Methods | EM (single particle) |
Resolution | 14.0 - 30.0 Å |
Structure data | EMDB-1327: EMDB-1328: EMDB-1329: EMDB-1330: EMDB-1331: EMDB-1332: |
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