New Insights into Ribosome Structure and Function

Cold Spring Harb Perspect Biol. 2019 Jan 2;11(1):a032615. doi: 10.1101/cshperspect.a032615.

Abstract

In the past 4 years, because of the advent of new cameras, many ribosome structures have been solved by cryoelectron microscopy (cryo-EM) at high, often near-atomic resolution, bringing new mechanistic insights into the processes of translation initiation, peptide elongation, termination, and recycling. Thus, cryo-EM has joined X-ray crystallography as a powerful technique in structural studies of translation. The significance of this new development is that structures of ribosomes in complex with their functional binding partners can now be determined to high resolution in multiple states as they perform their work. The aim of this article is to provide an overview of these new studies and assess the contributions they have made toward an understanding of translation and translational control.

Publication types

  • Review

MeSH terms

  • Animals
  • Bacteria / metabolism
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / metabolism
  • Fluorescence Resonance Energy Transfer
  • GTP Pyrophosphokinase / metabolism
  • Humans
  • Plasmodium falciparum / metabolism
  • Protein Binding
  • Protein Biosynthesis
  • Protein Conformation
  • Protein Transport
  • RNA, Transfer / metabolism
  • Ribosomes / chemistry*
  • Ribosomes / metabolism*
  • Trypanosoma / metabolism
  • Yeasts / metabolism

Substances

  • Escherichia coli Proteins
  • RNA, Transfer
  • GTP Pyrophosphokinase
  • relA protein, E coli