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Related Concept Videos

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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Cotranslational Protein Translocation01:20

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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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Post-translational Translocation of Proteins to the RER01:27

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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

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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

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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.
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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
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Related Experiment Video

Updated: Oct 2, 2025

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

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Ribosome exit tunnel electrostatics.

Marc Joiret1, Frederic Kerff2, Francesca Rapino3

  • 1Biomechanics Research Unit, GIGA In Silico Medicine, Liège University, CHU-B34(+5) 1 Avenue de l'Hôpital, 4000 Liège, Belgium.

Physical Review. E
|February 23, 2022
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Summary
This summary is machine-generated.

This study models ribosome exit tunnel electrostatics, revealing water molecules screen charges and tunnel features impede protein elongation. This impacts protein synthesis speed and cotranslational folding dynamics.

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Area of Science:

  • Molecular Biology
  • Biophysics
  • Structural Biology

Background:

  • Ribosome exit tunnel electrostatics' effect on protein elongation and nascent chain forces is poorly understood.
  • Previous studies measured electrostatic potential at limited points within the ribosome exit tunnel.

Purpose of the Study:

  • To develop a quantitative electrostatic model of the ribosome exit tunnel.
  • To describe interactions between nascent proteins and the tunnel at all points.
  • To elucidate the impact of electrostatics on protein synthesis dynamics.

Main Methods:

  • Developed a basic electrostatic model of the ribosome exit tunnel.
  • Quantitatively derived axial forces on nascent peptides at single-residue resolution.
  • Integrated data from molecular biology, crystallography, and physical chemistry.

Main Results:

  • Identified water molecules, not mobile ions, as primary electrostatic screeners via attraction to nucleic acid phosphates.
  • Demonstrated that tunnel wall composition and protein protrusions affect the electrostatic potential profile.
  • Showed that charged amino acid progression is impeded, altering elongation rates by -40% to +85%.

Conclusions:

  • The model quantitatively links experimental measurements to the ribosome's structural chemistry and tunnel geometry.
  • Findings provide insights into protein synthesis regulation and cotranslational protein folding.
  • The model serves as a tool for understanding ribosome mechanochemistry and translational control.