Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly

Nat Struct Mol Biol. 2015 Apr;22(4):342-344. doi: 10.1038/nsmb.2992. Epub 2015 Mar 16.

Abstract

We report crystal structures of the Thermus thermophilus ribosome at 2.3- to 2.5-Å resolution, which have enabled modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior stabilizing the functional fold of rRNA. Our work provides a resource to explore the roles of rRNA modifications and yields a more comprehensive atomic model of a bacterial ribosome.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Biosynthesis
  • Protein Structure, Tertiary
  • RNA, Bacterial / chemistry*
  • RNA, Messenger / chemistry
  • RNA, Ribosomal / chemistry*
  • RNA, Transfer / chemistry
  • Ribosomes / chemistry*
  • Thermus thermophilus / genetics*

Substances

  • RNA, Bacterial
  • RNA, Messenger
  • RNA, Ribosomal
  • RNA, Transfer

Associated data

  • PDB/4Y4O
  • PDB/4Y4P