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Related Concept Videos

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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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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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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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Improving Translational Accuracy02:07

Improving Translational Accuracy

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA...
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Articles linked to this work by shared authors, journal, and citation graph.

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Ribosome Structural Changes Dynamically Affect Ribosome Function.

International journal of molecular sciences·2024
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Inhibition of Ribosome Assembly and Ribosome Translation Has Distinctly Different Effects on Abundance and Paralogue Composition of Ribosomal Protein mRNAs in Saccharomyces cerevisiae.

mSystems·2023
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A Novel Model for the RNase MRP-Induced Switch between the Formation of Different Forms of 5.8S rRNA.

International journal of molecular sciences·2021
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Interaction between the assembly of the ribosomal subunits: Disruption of 40S ribosomal assembly causes accumulation of extra-ribosomal 60S ribosomal protein uL18/L5.

PloS one·2020
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Correction: The small and large ribosomal subunits depend on each other for stability and accumulation.

Life science alliance·2019
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Co-Assembly of 40S and 60S Ribosomal Proteins in Early Steps of Eukaryotic Ribosome Assembly.

International journal of molecular sciences·2019

Related Experiment Video

Updated: Sep 3, 2025

Rapid Isolation of the Mitoribosome from HEK Cells
09:33

Rapid Isolation of the Mitoribosome from HEK Cells

Published on: October 4, 2018

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Increasing Complexity of Ribosomes and Their Biogenesis.

Lasse Lindahl1

  • 1Department of Biological Sciences, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, USA.

International Journal of Molecular Sciences
|July 28, 2022
PubMed
Summary

The classic ribosome model views ribosomes solely as protein synthesis machinery. This perspective overlooks potential additional roles beyond translating genetic code into peptides.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The established ribosome model, originating from the 1960s-1970s, defines ribosomes as the cellular machinery responsible for protein synthesis.
  • This model posits that ribosomes translate the genetic information encoded in nucleic acids into the amino acid sequences of peptides.

Discussion:

  • The classic model emphasizes the ribosome's role in decoding the four-letter nucleic acid code into the 20-amino acid peptide code.
  • It highlights the involvement of transfer RNAs (tRNAs) and translation factors in this process, which are transiently associated with the ribosome.

Key Insights:

  • The traditional view limits the ribosome's function to translation and peptide polymerization.
  • This established model has been the cornerstone of understanding gene expression for decades.

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Last Updated: Sep 3, 2025

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Outlook:

  • Exploring potential non-canonical functions of ribosomes beyond protein synthesis.
  • Re-evaluating the ribosome's role in cellular processes may reveal new biological insights.