Identification of Two Distinct Hybrid State Intermediates on the Ribosome

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, quan...

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Bibliographic Details
Published in:Molecular cell 2007-02, Vol.25 (4), p.505-517
Main Authors: Munro, James B., Altman, Roger B., O'Connor, Nathan, Blanchard, Scott C.
Format: Article
Language:English
Subjects:
Acylation - drug effects
Escherichia coli - metabolism
Fluorescence Resonance Energy Transfer
Gene Deletion
Kinetics
Mutation - genetics
Nucleic Acid Conformation - drug effects
Peptides - metabolism
Puromycin - pharmacology
Ribosomal Proteins - genetics
Ribosomal Proteins - metabolism
Ribosomes - drug effects
Ribosomes - metabolism
RNA
RNA Stability - drug effects
RNA Transport
RNA, Ribosomal - metabolism
RNA, Transfer, Amino Acyl - chemistry
RNA, Transfer, Amino Acyl - metabolism
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Summary: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.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2007.01.022