Journal
EMBO JOURNAL
Volume 37, Issue 7, Pages -Publisher
WILEY
DOI: 10.15252/embj.201798499
Keywords
cryo-EM; pre-40S ribosome; ribosome; ribosome assembly; ribosome biogenesis
Categories
Funding
- Swiss National Science Foundation
- NCCR RNA AMP
- Disease, Novartis Foundation
- Olga Mayenfisch Stiftung
- European Research Council [EURIBIO260676]
- National Centre of Excellence in RNA and Disease project [138262]
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Final maturation of eukaryotic ribosomes occurs in the cytoplasm and requires the sequential removal of associated assembly factors and processing of the immature 20S pre-RNA. Using cryo-electron microscopy (cryo-EM), we have determined the structure of a yeast cytoplasmic pre-40S particle in complex with Enp1, Ltv1, Rio2, Tsr1, and Pno1 assembly factors poised to initiate final maturation. The structure reveals that the pre-rRNA adopts a highly distorted conformation of its 3' major and 3' minor domains stabilized by the binding of the assembly factors. This observation is consistent with a mechanism that involves concerted release of the assembly factors orchestrated by the folding of the rRNA in the head of the pre-40S subunit during the final stages of maturation. Our results provide a structural framework for the coordination of the final maturation events that drive a pre-40S particle toward the mature form capable of engaging in translation.
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