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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

11.1K
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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Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

1.0K
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...
1.0K
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

8.2K
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...
8.2K
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

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Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
3.1K
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.4K
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...
7.4K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

6.0K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
6.0K

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Related Experiment Video

Updated: Apr 12, 2026

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays
12:25

Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

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The Tat-dependent protein translocation pathway.

Bo Hou, Thomas Brüser

    Biomolecular Concepts
    |May 12, 2015
    PubMed
    Summary

    The twin-arginine translocation (Tat) pathway transports folded proteins across membranes using TatA and TatC proteins. Recent structural insights into Tat protein interactions have significant implications for understanding this essential biological process.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • The twin-arginine translocation (Tat) pathway facilitates the transport of folded proteins across biological membranes in various organisms.
    • This pathway is crucial for protein secretion in bacteria, archaea, and plant chloroplasts.
    • Tat pathway proteins, including TatA, TatB, and TatC, form large complexes involved in protein translocation.

    Purpose of the Study:

    • To summarize recent advances in understanding the structure and interactions of twin-arginine translocation pathway proteins.
    • To highlight the implications of these findings for the mechanism of protein transport.
    • To provide an overview of the components and variations of the Tat pathway across different life forms.

    Main Methods:

    • Review of recent structural and biochemical studies on Tat pathway components.

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    Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
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  • Analysis of protein-protein interactions within the Tat translocation machinery.
  • Comparative analysis of Tat pathway systems in different organisms.

    • Main Results:

    • The Tat pathway utilizes two main protein complexes, one involving TatC and the other TatA, which interact transiently during translocation.
    • TatB, present in some systems, is structurally related to TatA and often complexes with TatC.
    • Minimal two-component systems with a bifunctional TatA and TatC are also described.

    Conclusions:

    • Recent structural insights into Tat proteins and their interactions are crucial for understanding the mechanism of protein transport.
    • Variations in Tat pathway composition (two- vs. three-component systems) reflect evolutionary adaptations.
    • Further research into Tat protein structures and dynamics will illuminate fundamental aspects of transmembrane protein transport.