Extensions, Extra Factors, and Extreme Complexity: Ribosomal Structures Provide Insights into Eukaryotic Translation

Cold Spring Harb Perspect Biol. 2019 Sep 3;11(9):a032367. doi: 10.1101/cshperspect.a032367.


Although the basic aspects of protein synthesis are preserved in all kingdoms of life, there are many important structural and functional differences between bacterial and the more complex eukaryotic ribosomes. High-resolution cryo-electron microscopy (cryo-EM) and X-ray crystallography structures of eukaryotic ribosomes have revealed the complex architectures of eukaryotic ribosomes and species-specific variations in protein and ribosomal RNA (rRNA) extensions. They also enabled structural studies of a range of eukaryotic ribosomal complexes involved in translation initiation, elongation, and termination, revealing unique mechanistic features of the eukaryotic translation process, especially with respect to the identification and recognition of translation start and stop codons on messenger RNAs (mRNAs). Most recently, structural biology has provided insights into the eukaryotic ribosomal biogenesis pathway by visualizing several of its complex intermediates. This review highlights the past decade's structural work on eukaryotic ribosomes and its implications on our understanding of eukaryotic translation.

Publication types

  • Review

MeSH terms

  • Animals
  • CRISPR-Cas Systems*
  • Eukaryotic Cells / physiology*
  • Gene Editing
  • Genome, Archaeal
  • Genome, Bacterial
  • Models, Molecular
  • Phenotype
  • Protein Biosynthesis*
  • Protein Conformation
  • RNA Splicing
  • RNA, Long Noncoding / genetics
  • Ribosomes / physiology*
  • Transcription, Genetic


  • RNA, Long Noncoding