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Related Concept Videos

Ribosomes01:27

Ribosomes

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.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...
Ribosomes01:27

Ribosomes

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.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...
Ribosomes01:27

Ribosomes

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.
Ribosome Structure and Assembly
Ribosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within...
Ribosomes01:27

Ribosomes

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.Ribosome Structure and AssemblyRibosomes are composed of ribosomal RNA (rRNA) and proteins. In eukaryotes, rRNA is transcribed from genes in the nucleolus—a part of the nucleus that specializes in ribosome production. Within the...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...

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Updated: Jul 4, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
08:07

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

Spontaneous intersubunit rotation in single ribosomes.

Peter V Cornish1, Dmitri N Ermolenko, Harry F Noller

  • 1Department of Physics, University of Illinois, 1110 West Green Street, Urbana, IL 61801, USA.

Molecular Cell
|June 10, 2008
PubMed
Summary

Ribosomes spontaneously rotate between states during protein synthesis, a thermally driven process. This intersubunit rotation, crucial for translocation, is influenced by tRNA and elongation factor G.

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Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution
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Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution

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Last Updated: Jul 4, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

In Vitro Reassociation Assay to Measure the Formation of 80S Ribosomal Particles Using Salt-washed Ribosomal Subunits
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Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution
10:27

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution

Published on: July 8, 2019

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Ribosomal translocation is essential for protein synthesis, involving the movement of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
  • Elongation Factor G (EF-G) is known to catalyze this process, with previous studies suggesting a rotational mechanism between ribosomal subunits.

Purpose of the Study:

  • To investigate the role of intersubunit rotational movement in ribosomal translocation.
  • To determine the factors influencing this rotation and its thermal basis.

Main Methods:

  • Single-molecule Förster Resonance Energy Transfer (smFRET) was employed to observe ribosome dynamics.
  • Ribosomes were studied in various states, including pretranslocation and posttranslocation, with and without EF-G and different tRNA acylation states.

Main Results:

  • Pretranslocation ribosomes exhibit spontaneous intersubunit rotation, fluctuating between classical and hybrid states, even without EF-G.
  • Posttranslocation ribosomes are primarily in a non-rotated classical state.
  • Binding of EF-G and the movement of deacylated tRNA into the E site stabilize the rotated hybrid state.
  • The acylation state of tRNA in the P site significantly impacts the frequency of intersubunit rotation.

Conclusions:

  • Ribosomal intersubunit rotation is a thermally driven process underlying translocation.
  • This rotation is not solely dependent on EF-G but is influenced by tRNA binding and ribosome state.