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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Codon-dependent tRNA fluctuations monitored with fluorescence polarization.

Padmaja P Mishra1, Mohd Tanvir Qureshi, Wenhui Ren

  • 1Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA.

Biophysical Journal
|November 30, 2010
PubMed
Summary
This summary is machine-generated.

Ribosomes accurately select aminoacyl-tRNA (aa-tRNA) during protein synthesis. This study reveals cognate aa-tRNA fluctuates less than near-cognate, suggesting an induced-fit mechanism guides accurate selection.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Structural Biology

Background:

  • Ribosomes accurately select aminoacyl-tRNA (aa-tRNA) during protein synthesis based on mRNA codons.
  • The precise mechanism governing this high-fidelity selection remains largely unknown.

Purpose of the Study:

  • To investigate the dynamics of tRNA within the ribosome during selection.
  • To elucidate the mechanism underlying cognate versus near-cognate aa-tRNA discrimination.

Main Methods:

  • Single-molecule fluorescence resonance energy transfer (smFRET).
  • Fluorescence emission anisotropy.
  • Nanosecond timescale dynamics analysis.

Main Results:

  • Observed random thermal motion (fluctuations) of tRNAs within the ribosome on a nanosecond timescale.
  • Cognate aa-tRNA exhibits less frequent fluctuations compared to near-cognate aa-tRNA.
  • Cognate and near-cognate aa-tRNAs occupy similar positions within the ribosome.

Conclusions:

  • The reduced fluctuation of cognate aa-tRNA suggests a guiding mechanism for accurate selection.
  • An induced-fit mechanism involving the 30S ribosomal subunit upon cognate aa-tRNA binding is proposed.
  • A mechanistic model for GTP hydrolysis by elongation factor Tu mediated by aa-tRNA was suggested.