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Related Concept Videos

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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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.
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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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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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Termination of Translation01:44

Termination of Translation

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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Structural Heterogeneity in Pre-40S Ribosomes.

Matthew C Johnson1, Homa Ghalei2, Katelyn A Doxtader2

  • 1Department of Biological Science, Institute of Molecular Biophysics, Florida State University, 91 Chieftain Way, Tallahassee, FL 32306, USA.

Structure (London, England : 1993)
|January 24, 2017
PubMed
Summary
This summary is machine-generated.

Late-stage ribosome assembly involves seven factors (AFs) with unknown mechanisms. New cryo-EM structures reveal extensive heterogeneity in assembly factors, regulating subunit joining and maturation.

Keywords:
cryo-EMpre-40S ribosomeribosome assemblyribosome biogenesissmall subunit assembly

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Late-stage 40S ribosome assembly is a complex cytoplasmic process crucial for protein synthesis.
  • Seven essential assembly factors (AFs) orchestrate ribosome maturation, but their precise roles remain largely undefined.
  • Understanding these mechanisms is vital for comprehending gene expression and cellular function.

Purpose of the Study:

  • To elucidate the structural mechanisms of late-stage 40S ribosome assembly.
  • To investigate the role of assembly factors in regulating ribosome maturation and subunit joining.
  • To provide high-resolution structural insights into previously unresolved regions of the pre-40S subunit.

Main Methods:

  • Three-dimensional (3D) cryoelectron microscopy (cryo-EM) was employed to determine structures of the immature small subunit (pre-40S).
  • Advanced 3D sorting techniques were utilized to analyze the structural heterogeneity of the pre-40S particle.
  • Biochemical analyses, including point variant studies, were performed to validate structural models.

Main Results:

  • Cryo-EM structures revealed extensive structural heterogeneity among interface assembly factors during 40S maturation.
  • High-resolution models were generated for the beak and platform regions of the pre-40S subunit.
  • Evidence suggests Dim1 dissociation from the subunit interface regulates the maturation of the 18S rRNA 3' end.

Conclusions:

  • Structural heterogeneity of assembly factors plays a key role in regulating subunit joining during 40S ribosome maturation.
  • The structural models provide new insights into the function of AFs and rRNA localization in specific ribosome regions.
  • The dissociation of Dim1 is identified as a critical step in the final maturation of the 18S rRNA 3' end.