Cryo-electron microscopy of ribosomal complexes in cotranslational folding, targeting, and translocation

Kèvin Knoops, Guy Schoehn, Christiane Schaffitzel

Research output: Contribution to journalArticle (Academic Journal)peer-review

10 Citations (Scopus)


Single-particle cryo-electron microscopy (cryo-EM) became a well-established method to study the structure and function of large macromolecular assemblies in a close to physiological environment. Cryo-EM reconstructions of ribosomal complexes trapped at different stages during translation, cotranslational targeting, and translocation provide new insights on a molecular level into these processes, which are vital for the correct localization and folding of all proteins in the cell. The EM structures in combination with biochemical experiments and available high-resolution crystal or nuclear magnetic resonance (NMR) structures of individual factors and of the ribosome allow for interpretation in quasi-atomic detail of the molecular mechanism of ribosomal complexes, their conformational changes and dynamic interactions with factors like the signal recognition particle, SRP receptor, the translocon, and the chaperone trigger factor. The snapshots obtained by single-particle EM reconstructions enable us to follow the path of a nascent protein from the peptidyl-transferase center, through the ribosomal tunnel, to and across the translocon in the membrane. With new developments in image processing techniques it is possible to sort a biological homogenous sample into different conformational states and to reach subnanometer resolution such that folding of the nascent chain into secondary structure elements can be directly visualized. With improved cryo-electron tomography and correlative light microscopy and EM, it will be possible to visualize ribosomal complexes in their cellular context.

Original languageEnglish
Pages (from-to)429-41
Number of pages13
JournalWiley Interdisciplinary Reviews: RNA
Issue number3
Publication statusPublished - 19 Nov 2011

Bibliographical note

Copyright © 2011 John Wiley & Sons, Ltd.


  • Cryoelectron Microscopy
  • Models, Molecular
  • Peptidyl Transferases
  • Protein Biosynthesis
  • RNA, Transfer
  • Ribosomes


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