Related Experiment Video
Updated: Mar 22, 2026

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
Published on: February 21, 2019
Twin-Arginine Protein Translocation.
Vivianne J Goosens1, Jan Maarten van Dijl2
1MRC Centre for Molecular Bacteriology and Infection, Section of Microbiology, Imperial College London, London, SW7 2AZ, UK.
The twin-arginine translocation (Tat) system in Gram-positive bacteria moves folded proteins across membranes. This review details Tat pathway components, mechanisms, and its potential in biotechnology and as an antimicrobial target.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Twin-arginine translocation (Tat) systems are essential for transporting folded proteins across cellular membranes.
- These systems are crucial in Gram-positive bacteria for protein secretion.
Purpose of the Study:
- To review the composition and mechanistic aspects of the Tat pathway in Gram-positive bacteria.
- To highlight the Tat pathway's role in protein translocation, cofactor incorporation, and protein folding.
- To discuss the Tat pathway's potential applications in biotechnology and as an antimicrobial target.
Main Methods:
- Literature review focusing on Tat pathways in Gram-positive bacteria.
- Analysis of Tat pathway components (TatA, TatC) and their interactions.
- Examination of cargo protein translocation mechanisms and cofactor requirements.
Main Results:
- The minimal Tat pathway consists of TatA and TatC, often with additional TatA-like proteins.
- Tat pathways exhibit flexibility, ensuring correct protein folding and cofactor incorporation.
- Specific features of Tat pathways in various Gram-positive bacteria, including Bacillus subtilis, are detailed.
Conclusions:
- Understanding Gram-positive bacterial Tat pathways is crucial for various applications.
- The Tat system offers potential for biotechnological protein secretion and antimicrobial drug development.
Related Concept Videos
Cotranslational Protein Translocation
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...
Protein Translocation Machinery on 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...
Protein Transport to the Thylakoids
Translocation of Proteins into the Mitochondria
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Bacterial Translocation and Protein Secretion
Protein Transport into the Inner Mitochondrial Membrane
Transport of mitochondrial precursors across the TIM23 channel is driven by...

