期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 104, 期 14, 页码 5788-5793出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0606880104
关键词
posttranscriptional gene expression; protein synthesis; ribosome structure
资金
- Biotechnology and Biological Sciences Research Council [BB/D524608/1] Funding Source: researchfish
- Medical Research Council [G0500365] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/D524608/1] Funding Source: Medline
- Medical Research Council [G0500365] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
- BBSRC [BB/D524608/1] Funding Source: UKRI
- MRC [G0500365] Funding Source: UKRI
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 (eIF's). 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.
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