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-Structure paper
タイトル | Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 24, Issue 5, Page 453-460, Year 2017 |
掲載日 | 2017年4月3日 |
著者 | André Heuer / Milan Gerovac / Christian Schmidt / Simon Trowitzsch / Anne Preis / Peter Kötter / Otto Berninghausen / Thomas Becker / Roland Beckmann / Robert Tampé / |
PubMed 要旨 | The essential ATP-binding cassette protein ABCE1 splits 80S ribosomes into 60S and 40S subunits after canonical termination or quality-control-based mRNA surveillance processes. However, the ...The essential ATP-binding cassette protein ABCE1 splits 80S ribosomes into 60S and 40S subunits after canonical termination or quality-control-based mRNA surveillance processes. However, the underlying splitting mechanism remains enigmatic. Here, we present a cryo-EM structure of the yeast 40S-ABCE1 post-splitting complex at 3.9-Å resolution. Compared to the pre-splitting state, we observe repositioning of ABCE1's iron-sulfur cluster domain, which rotates 150° into a binding pocket on the 40S subunit. This repositioning explains a newly observed anti-association activity of ABCE1. Notably, the movement implies a collision with A-site factors, thus explaining the splitting mechanism. Disruption of key interactions in the post-splitting complex impairs cellular homeostasis. Additionally, the structure of a native post-splitting complex reveals ABCE1 to be part of the 43S initiation complex, suggesting a coordination of termination, recycling, and initiation. |
リンク | Nat Struct Mol Biol / PubMed:28368393 |
手法 | EM (単粒子) |
解像度 | 3.9 - 14.0 Å |
構造データ | EMDB-3452: |
化合物 | ChemComp-SF4: ChemComp-ANP: ChemComp-MG: |
由来 |
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キーワード | RIBOSOME (リボソーム) / ABCE1 / recycling (リサイクル) / 40S |