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Related Concept Videos

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Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
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Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that synthesize large quantities of protein—such as secretory cells in the human pancreas—can contain millions of ribosomes.
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Related Experiment Video

Updated: Jun 3, 2025

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Capturing eukaryotic ribosome dynamics in situ at high resolution.

Jing Cheng1, Chunling Wu1, Junxi Li1,2

  • 1Key Laboratory of Biomacromolecules (CAS), National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.

Nature Structural & Molecular Biology
|January 9, 2025
PubMed
Summary

Researchers visualized over 20 distinct ribosome conformations during eukaryotic translation elongation using cryo-electron microscopy. This detailed map reveals how elongation factors (eEFs) interact with the ribosome to facilitate protein synthesis.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Protein complexes, such as ribosomes, are highly dynamic in cells.
  • Understanding these conformational changes is essential for elucidating cellular functions.

Purpose of the Study:

  • To characterize the dynamic conformational changes of the Saccharomyces cerevisiae ribosome during eukaryotic translation elongation.
  • To visualize the roles of elongation factors (eEFs) in different ribosomal states.

Main Methods:

  • In situ single-particle cryo-electron microscopy (cryo-EM) of Saccharomyces cerevisiae cell lamellae.
  • Acquisition of 451,700 ribosome particles.
  • Three-dimensional classification to resolve distinct conformations.

Main Results:

  • Solved the 60S ribosomal subunit structure to 2.9-Å resolution and identified over 20 distinct conformations at resolutions typically higher than 4 Å.
  • Reconstructed a complete eukaryotic translation elongation cycle.
  • Observed compact eEF2 stabilizing the ribosome for peptidyl transfer and open-eEF3 binding to a fully rotated ribosome, coupled with 40S subunit movements.

Conclusions:

  • The study provides a high-resolution dynamic map of the eukaryotic translation elongation cycle.
  • Elongation factors eEF2 and eEF3 play distinct roles in stabilizing specific ribosomal conformations during translation.
  • These findings offer insights into the intricate mechanisms of protein synthesis.