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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

10.9K
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...
10.9K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

8.0K
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...
8.0K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.2K
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...
7.2K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.9K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
2.9K
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

965
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
965
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

5.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
5.1K

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Related Experiment Video

Updated: Mar 19, 2026

Measuring Peptide Translocation into Large Unilamellar Vesicles
12:27

Measuring Peptide Translocation into Large Unilamellar Vesicles

Published on: January 27, 2012

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Protein translocation: what's the problem?

Robin A Corey1, William J Allen1, Ian Collinson2

  • 1School of Biochemistry, University of Bristol, University Walk, BS8 1TD, U.K.

Biochemical Society Transactions
|June 11, 2016
PubMed
Summary
This summary is machine-generated.

Researchers propose a new hypothesis for protein translocation through the Sec system, a vital biological process. This review examines alternative models, offering insights into molecular mechanisms of protein transport.

Keywords:
ATPaseSecYenergy transductionmembrane protein complexprotein translocationsecretion

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Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
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Area of Science:

  • Molecular Biology
  • Biochemistry

Background:

  • The Sec system is essential for protein translocation across cellular membranes.
  • Understanding the molecular mechanisms of protein transport is crucial for cell biology.

Purpose of the Study:

  • To present a novel hypothesis for the molecular mechanism of protein translocation via the Sec system.
  • To review and analyze existing alternative and contested models of protein translocation.

Main Methods:

  • Hypothesis generation based on years of research collaboration.
  • Analysis of existing data and literature on protein translocation models.
  • Review of bacterial secretion processes as a model system.

Main Results:

  • A new hypothesis for the Sec system's protein translocation mechanism is proposed.
  • Pros and cons of alternative protein translocation models are discussed.
  • Progress in understanding protein translocation is highlighted.

Conclusions:

  • The proposed hypothesis offers a potential advancement in understanding protein translocation.
  • Further research and validation of the new model are warranted.
  • The review provides a comprehensive overview of current models in the field.