The central role of protein S12 in organizing the structure of the decoding site of the ribosome. Academic Article uri icon

Overview

MeSH

  • Amino Acid Substitution
  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli
  • Models, Molecular
  • Nucleic Acid Conformation
  • Point Mutation
  • Protein Binding
  • Protein Subunits
  • RNA, Transfer, Phe
  • Ribosomes

MeSH Major

  • Bacterial Proteins
  • Ribosomal Proteins
  • Thermus thermophilus

abstract

  • The ribosome decodes mRNA by monitoring the geometry of codon-anticodon base-pairing using a set of universally conserved 16S rRNA nucleotides within the conformationally dynamic decoding site. By applying single-molecule FRET and X-ray crystallography, we have determined that conditional-lethal, streptomycin-dependence mutations in ribosomal protein S12 interfere with tRNA selection by allowing conformational distortions of the decoding site that impair GTPase activation of EF-Tu during the tRNA selection process. Distortions in the decoding site are reversed by streptomycin or by a second-site suppressor mutation in 16S rRNA. These observations encourage a refinement of the current model for decoding, wherein ribosomal protein S12 and the decoding site collaborate to optimize codon recognition and substrate discrimination during the early stages of the tRNA selection process.

publication date

  • December 2013

has subject area

  • Amino Acid Substitution
  • Bacterial Proteins
  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli
  • Models, Molecular
  • Nucleic Acid Conformation
  • Point Mutation
  • Protein Binding
  • Protein Subunits
  • RNA, Transfer, Phe
  • Ribosomal Proteins
  • Ribosomes
  • Thermus thermophilus

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3884664

Digital Object Identifier (DOI)

  • 10.1261/rna.040030.113

PubMed ID

  • 24152548

Additional Document Info

start page

  • 1791

end page

  • 1801

volume

  • 19

number

  • 12