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-Structure paper
タイトル | Ribosome assembly factors prevent premature translation initiation by 40S assembly intermediates. |
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ジャーナル・号・ページ | Science, Vol. 333, Issue 6048, Page 1449-1453, Year 2011 |
掲載日 | 2011年9月9日 |
著者 | Bethany S Strunk / Cherisse R Loucks / Min Su / Harish Vashisth / Shanshan Cheng / Justin Schilling / Charles L Brooks / Katrin Karbstein / Georgios Skiniotis / |
PubMed 要旨 | Ribosome assembly in eukaryotes requires approximately 200 essential assembly factors (AFs) and occurs through ordered events that initiate in the nucleolus and culminate in the cytoplasm. Here, we ...Ribosome assembly in eukaryotes requires approximately 200 essential assembly factors (AFs) and occurs through ordered events that initiate in the nucleolus and culminate in the cytoplasm. Here, we present the electron cryo-microscopy (cryo-EM) structure of a late cytoplasmic 40S ribosome assembly intermediate from Saccharomyces cerevisiae at 18 angstrom resolution. We obtained cryo-EM reconstructions of preribosomal complexes lacking individual components to define the positions of all seven AFs bound to this intermediate. These late-binding AFs are positioned to prevent each step in the translation initiation pathway. Together, they obstruct the binding sites for initiation factors, prevent the opening of the messenger RNA channel, block 60S subunit joining, and disrupt the decoding site. These redundant mechanisms probably ensure that pre-40S particles do not enter the translation pathway, which would result in their rapid degradation. |
リンク | Science / PubMed:21835981 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 18.0 - 30.0 Å |
構造データ | EMDB-1922: EMDB-1923: EMDB-1924: EMDB-1925: EMDB-1926: EMDB-1927: |
由来 |
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