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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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Related Experiment Video

Updated: Jun 6, 2026

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

Published on: December 16, 2025

Interdependencies govern multidomain architecture in ribosomal small subunit assembly.

Deepika Calidas1, Gloria M Culver

  • 1Department of Biology, University of Rochester, Rochester, New York 14627, USA.

RNA (New York, N.Y.)
|December 16, 2010
PubMed
Summary

Ribosomal protein S8 monitors 30S subunit assembly. Its binding site structure is similar to the mature subunit, but other protein interactions reveal complex domain assembly dependencies.

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Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
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Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Related Experiment Videos

Last Updated: Jun 6, 2026

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

Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling
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Global Identification of Co-Translational Interaction Networks by Selective Ribosome Profiling

Published on: October 7, 2021

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The 30S ribosomal subunit's functional integrity relies on the precise assembly and orientation of its four structural domains.
  • Understanding the assembly process is crucial for comprehending protein synthesis and ribosome function.

Purpose of the Study:

  • To investigate conformational changes in 16S rRNA during in vitro 30S subunit assembly.
  • To utilize directed hydroxyl radical probing with Fe(II)-derivatized ribosomal protein S8 (r-protein S8) to monitor domain orientation.

Main Methods:

  • Employing Fe(II)-derivatized r-protein S8 to mediate hydroxyl radical probing of 16S rRNA.
  • Comparing cleavage patterns in minimal ribonucleoprotein (RNP) particles with those in the fully assembled 30S subunit.

Main Results:

  • R-protein S8's primary binding site at helix 21 maintains a mature-like structure independent of other proteins.
  • R-protein S8's secondary binding site at helices 25-26a shows altered cleavage intensities depending on the presence of other r-proteins.
  • Assembly of the 30S body domain influences the architecture of helix 12 and the 5' terminus, while neck assembly depends on both head and body assembly.

Conclusions:

  • The assembly of the 30S subunit involves intricate interdependencies between the assembly of individual domains and the incorporation of key ribosomal proteins.
  • R-protein S8 serves as a valuable probe for dissecting the spatial relationships and conformational dynamics during 30S subunit biogenesis.