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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 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...
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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Related Experiment Video

Updated: Jun 7, 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

Visualizing ribosome biogenesis: parallel assembly pathways for the 30S subunit.

Anke M Mulder1, Craig Yoshioka, Andrea H Beck

  • 1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Science (New York, N.Y.)
|October 30, 2010
PubMed
Summary
This summary is machine-generated.

Researchers mapped the intricate assembly of the 30S ribosomal subunit using discovery single-particle profiling (DSP). This revealed a multi-step mechanism for ribosome biogenesis, detailing intermediate structures and their dynamics.

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Last Updated: Jun 7, 2026

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

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Published on: July 6, 2021

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08:49

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Published on: March 16, 2016

In Vitro Reassociation Assay to Measure the Formation of 80S Ribosomal Particles Using Salt-washed Ribosomal Subunits
06:09

In Vitro Reassociation Assay to Measure the Formation of 80S Ribosomal Particles Using Salt-washed Ribosomal Subunits

Published on: December 16, 2025

Area of Science:

  • Molecular Biology
  • Cellular Physiology
  • Structural Biology

Background:

  • Ribosomes are essential macromolecular machines responsible for protein synthesis via DNA translation.
  • Understanding ribosome biogenesis is crucial for cellular physiology, yet the assembly pathways remain mechanistically unclear.
  • Previous studies suggested parallel assembly pathways for the Escherichia coli 30S subunit, lacking detailed mechanistic insights.

Purpose of the Study:

  • To elucidate the mechanism of 30S ribosomal subunit assembly in Escherichia coli.
  • To identify and structurally characterize assembly intermediates and their population dynamics.
  • To construct a comprehensive model of ribosome biogenesis incorporating kinetic and structural data.

Main Methods:

  • Employed discovery single-particle profiling (DSP), a time-resolved electron microscopy technique.
  • Acquired over one million snapshots of assembling 30S subunits.
  • Integrated DSP data with mass spectrometry for a multi-faceted mechanistic analysis.

Main Results:

  • Identified and visualized the structures of 14 distinct assembly intermediates.
  • Monitored the population flux and dynamics of these intermediates over time.
  • Developed the first detailed ribosome-assembly mechanism, including binding dependencies and rate constants.

Conclusions:

  • The study provides a comprehensive mechanistic model for 30S ribosomal subunit assembly.
  • DSP is a powerful tool for dissecting complex macromolecular assembly processes.
  • The findings advance our understanding of ribosome biogenesis and cellular function.