Structural basis for the control of translation initiation during stress

Nat Struct Mol Biol. 2004 Nov;11(11):1054-9. doi: 10.1038/nsmb850. Epub 2004 Oct 24.


During environmental stress, organisms limit protein synthesis by storing inactive ribosomes that are rapidly reactivated when conditions improve. Here we present structural and biochemical data showing that protein Y, an Escherichia coli stress protein, fills the tRNA- and mRNA-binding channel of the small ribosomal subunit to stabilize intact ribosomes. Protein Y inhibits translation initiation during cold shock but not at normal temperatures. Furthermore, protein Y competes with conserved translation initiation factors that, in bacteria, are required for ribosomal subunit dissociation. The mechanism used by protein Y to reduce translation initiation during stress and quickly release ribosomes for renewed translation initiation may therefore occur widely in nature.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins
  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Escherichia coli Proteins
  • Models, Biological
  • Models, Molecular
  • Protein Biosynthesis*
  • RNA, Messenger / metabolism
  • RNA, Transfer / metabolism
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / physiology*
  • Ribosomes / chemistry
  • Ribosomes / metabolism
  • Ribosomes / ultrastructure
  • Temperature
  • X-Rays


  • Bacterial Proteins
  • Escherichia coli Proteins
  • RNA, Messenger
  • RaiA protein, E coli
  • Ribosomal Proteins
  • YfiA protein, bacteria
  • RNA, Transfer

Associated data

  • PDB/14LS
  • PDB/1GIX
  • PDB/1HR0
  • PDB/IVP0