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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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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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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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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Related Experiment Video

Updated: Mar 19, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
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Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

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Insights into Cotranslational Nascent Protein Behavior from Computer Simulations.

Fabio Trovato1, Edward P O'Brien1

  • 1Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802;

Annual Review of Biophysics
|June 15, 2016
PubMed
Summary

Protein synthesis regulation is key for cellular function and disease. Molecular simulations reveal how ribosome speed impacts cotranslational processes, offering new insights into protein folding and disease mechanisms.

Keywords:
biomolecular modelingcotranslational processesmolecular simulationsnascent proteinsynonymous mutationstranslation rate

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Related Experiment Videos

Last Updated: Mar 19, 2026

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA
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Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology

Background:

  • Protein stability and function are regulated during synthesis (translation) by ribosomes.
  • Cotranslational processes like folding, modification, and secretion are influenced by the ribosome's amino acid addition rate.
  • Altered translation rates are linked to diseases, including cancer.

Purpose of the Study:

  • To review recent insights into cotranslational processes.
  • To discuss the integration of computational approaches for understanding these processes.
  • To highlight new discoveries from molecular simulations.

Main Methods:

  • Review of molecular simulation studies.
  • Integration of multi-scale computational approaches.
  • Analysis of experimental data on translation rates.

Main Results:

  • Molecular simulations provide detailed insights into cotranslational folding and interactions.
  • Multi-scale computational methods reveal complex dynamics of nascent polypeptide chains.
  • Simulation data illuminates how translation speed affects protein biogenesis and disease links.

Conclusions:

  • Computational approaches are crucial for understanding cotranslational processes.
  • Future research should leverage simulations to explore remaining questions in protein synthesis and disease.
  • Further investigation into translation dynamics can uncover novel therapeutic targets.