Identification of two distinct hybrid state intermediates on the ribosome. Academic Article uri icon

Overview

MeSH

  • Acylation
  • Fluorescence Resonance Energy Transfer
  • Gene Deletion
  • Kinetics
  • Mutation
  • Peptides
  • Puromycin
  • RNA Stability
  • RNA Transport
  • RNA, Ribosomal
  • Ribosomal Proteins

MeSH Major

  • Escherichia coli
  • Nucleic Acid Conformation
  • RNA, Transfer, Amino Acyl
  • Ribosomes

abstract

  • High spatial and time resolution single-molecule fluorescence resonance energy transfer measurements have been used to probe the structural and kinetic parameters of transfer RNA (tRNA) movements within the aminoacyl (A) and peptidyl (P) sites of the ribosome. Our investigation of tRNA motions, quantified on wild-type, mutant, and L1-depleted ribosome complexes, reveals a dynamic exchange between three metastable tRNA configurations, one of which is a previously unidentified hybrid state in which only deacylated-tRNA adopts its hybrid (P/E) configuration. This new dynamic information suggests a framework in which the formation of intermediate states in the translocation process is achieved through global conformational rearrangements of the ribosome particle.

publication date

  • February 23, 2007

has subject area

  • Acylation
  • Escherichia coli
  • Fluorescence Resonance Energy Transfer
  • Gene Deletion
  • Kinetics
  • Mutation
  • Nucleic Acid Conformation
  • Peptides
  • Puromycin
  • RNA Stability
  • RNA Transport
  • RNA, Ribosomal
  • RNA, Transfer, Amino Acyl
  • Ribosomal Proteins
  • Ribosomes

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC2244649

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2007.01.022

PubMed ID

  • 17317624

Additional Document Info

start page

  • 505

end page

  • 517

volume

  • 25

number

  • 4