Insights into remodeling events during eukaryotic large ribosomal subunit assembly provided by high resolution cryo-EM structures

RNA Biol. 2017 Oct 3;14(10):1306-1313. doi: 10.1080/15476286.2017.1297914. Epub 2017 Mar 7.

Abstract

Ribosomes are responsible for translating the genome, in the form of mRNA, into the proteome in all organisms. Biogenesis of ribosomes in eukaryotes is a complex process involving numerous remodeling events driven in part by the concerted actions of hundreds of protein assembly factors. A major challenge in studying eukaryotic ribosome assembly has, until recently, been a lack of structural data to facilitate understanding of the conformational and compositional changes the pre-ribosome undergoes during its construction. Cryo-electron microscopy (cryo-EM) has begun filling these gaps; recent advances in cryo-EM have enabled the determination of several high resolution pre-ribosome structures. This review focuses mainly on lessons learned from the study of pre-60S particles purified from yeast using the assembly factor Nog2 as bait. These Nog2 particles provide insight into many aspects of nuclear stages of 60S subunit assembly, including construction of major 60S subunit functional centers and processing of the ITS2 spacer RNA.

Keywords: Assembly intermediates; high resolution cryo-EM; remodeling; ribosome biogenesis.

Publication types

  • Review

MeSH terms

  • Cryoelectron Microscopy
  • DNA, Ribosomal Spacer
  • GTP Phosphohydrolases / metabolism*
  • Models, Molecular
  • Protein Biosynthesis
  • Protein Conformation
  • Protein Multimerization
  • Ribosome Subunits, Large, Eukaryotic / chemistry*
  • Ribosome Subunits, Large, Eukaryotic / metabolism*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • DNA, Ribosomal Spacer
  • Saccharomyces cerevisiae Proteins
  • GTP Phosphohydrolases
  • NOG2 protein, S cerevisiae