Architecture of the 90S pre-ribosome: a structural view on the birth of the eukaryotic ribosome
The 90S pre-ribosome is an early biogenesis intermediate formed during co-transcriptional ribosome formation, composed of ∼70 assembly factors and several small nucleolar RNAs (snoRNAs) that associate with nascent pre-rRNA. We report the cryo-EM structure of the Chaetomium thermophilum 90S pre-ribos...
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| Hauptverfasser: | , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
14 July 2016
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| In: |
Cell
Year: 2016, Jahrgang: 166, Heft: 2, Pages: 380-393 |
| ISSN: | 1097-4172 |
| DOI: | 10.1016/j.cell.2016.06.014 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.cell.2016.06.014 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0092867416307437 
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| Verfasserangaben: | Markus Kornprobst, Martin Turk, Nikola Kellner, Jingdong Cheng, Dirk Flemming, Isabelle Koš-Braun, Martin Koš, Matthias Thoms, Otto Berninghausen, Roland Beckmann, and Ed Hurt |
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| 520 | |a The 90S pre-ribosome is an early biogenesis intermediate formed during co-transcriptional ribosome formation, composed of ∼70 assembly factors and several small nucleolar RNAs (snoRNAs) that associate with nascent pre-rRNA. We report the cryo-EM structure of the Chaetomium thermophilum 90S pre-ribosome, revealing how a network of biogenesis factors including 19 β-propellers and large α-solenoid proteins engulfs the pre-rRNA. Within the 90S pre-ribosome, we identify the UTP-A, UTP-B, Mpp10-Imp3-Imp4, Bms1-Rcl1, and U3 snoRNP modules, which are organized around 5′-ETS and partially folded 18S rRNA. The U3 snoRNP is strategically positioned at the center of the 90S particle to perform its multiple tasks during pre-rRNA folding and processing. The architecture of the elusive 90S pre-ribosome gives unprecedented structural insight into the early steps of pre-rRNA maturation. Nascent rRNA that is co-transcriptionally folded and given a particular shape by encapsulation within a dedicated mold-like structure is reminiscent of how polypeptides use chaperone chambers for their protein folding. | ||
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