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Related Concept Videos

Ribosomes01:27

Ribosomes

75.4K
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...
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Ribosomes01:27

Ribosomes

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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.
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...
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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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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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Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

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No description available
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Ribosome Profiling02:24

Ribosome Profiling

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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.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
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Initiation of Translation02:33

Initiation of Translation

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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Related Experiment Video

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Assessment of DNA Contamination in RNA Samples Based on Ribosomal DNA
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A computer model for the 30S ribosome subunit

I D Kuntz, G M Crippen

    Biophysical Journal
    |November 1, 1980
    PubMed
    Summary

    A new computational model maps the 21 proteins of the E. coli 30S ribosomal subunit using distance geometry. This approach integrates experimental data to define protein locations within the ribosome structure.

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Computational Biology

    Background:

    • The E. coli ribosome is crucial for protein synthesis.
    • Understanding the precise arrangement of ribosomal proteins is key to deciphering its function.
    • Previous models often simplified protein representations.

    Purpose of the Study:

    • To develop a computer-generated model of the E. coli 30S ribosomal subunit.
    • To precisely map the locations of all 21 constituent proteins.
    • To integrate diverse experimental data for a more accurate structural representation.

    Main Methods:

    • Utilized distance geometry, a mathematical technique, to model protein locations.
    • Incorporated experimental data from immunoelectron microscopy.

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    Chromatographic Purification of Highly Active Yeast Ribosomes
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  • Integrated data from neutron-scattering studies.
  • Treated proteins as extended structures, not just centers of mass.
  • Constrained solutions to fit an approximate 30S subunit boundary surface.

    • Main Results:

    • Generated a self-consistent model for the locations of 21 proteins in the 30S subunit.
    • Achieved well-defined structures with protein coordinate variations of approximately 20 Å.
    • Successfully confined protein locations within a defined boundary, respecting the overall 30S shape.

    Conclusions:

    • The developed model provides a refined structural map of the E. coli 30S ribosomal subunit.
    • The integration of experimental data and advanced computational methods yields accurate protein positioning.
    • This model serves as a valuable resource for further studies on ribosome structure and function.