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-Structure paper
タイトル | Cotranslational Protein Folding inside the Ribosome Exit Tunnel. |
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ジャーナル・号・ページ | Cell Rep, Vol. 12, Issue 10, Page 1533-1540, Year 2015 |
掲載日 | 2015年9月8日 |
著者 | Ola B Nilsson / Rickard Hedman / Jacopo Marino / Stephan Wickles / Lukas Bischoff / Magnus Johansson / Annika Müller-Lucks / Fabio Trovato / Joseph D Puglisi / Edward P O'Brien / Roland Beckmann / Gunnar von Heijne / |
PubMed 要旨 | At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel ...At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of cotranslational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins. |
リンク | Cell Rep / PubMed:26321634 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.8 Å |
構造データ | |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | TRANSLATION / PROTEIN FOLDING / RIBOSOME / ZINC FINGER / SECM / TRANSLATIONAL ARREST PEPTIDE / CRYO-EM / SINGLE- MOLECULE STUDIES |