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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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 translocon complex.
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

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Related Experiment Video

Updated: Jun 24, 2026

F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
07:09

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

Published on: March 16, 2022

From the Sec complex to the membrane insertase YidC.

Andreas Kuhn1

  • 1Institute of Microbiology and Molecular Biology, University of Hohenheim, D-70593 Stuttgart, Germany. andikuhn@uni-hohenheim.de

Biological Chemistry
|April 14, 2009
PubMed
Summary
This summary is machine-generated.

The Sec translocase and YidC membrane insertase enzymes guide protein insertion into cell membranes. Molecular insights reveal specific interactions forming a pathway for newly synthesized proteins to enter and cross the membrane bilayer.

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F&#246;rster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
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Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs

Published on: November 19, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein insertion into cellular membranes is crucial for cell function.
  • The Sec translocase and YidC membrane insertase are key enzymes involved in this process.

Purpose of the Study:

  • To provide a molecular understanding of how Sec translocase and YidC facilitate protein membrane insertion.
  • To elucidate the interactions and pathway involved in protein translocation across the membrane bilayer.

Main Methods:

  • Structural biology insights
  • Functional intermediate analysis
  • Molecular interaction studies

Main Results:

  • Detailed molecular glimpse into the mechanism of protein insertion.
  • Identification of specific protein interactions in the cytoplasm and at the membrane surface.
  • Characterization of a defined pathway for membrane protein movement.

Conclusions:

  • Sec translocase and YidC act in concert to insert proteins into membranes.
  • Specific molecular interactions define a route for protein translocation.
  • Understanding these mechanisms is key to comprehending membrane protein biogenesis.