scholarly journals Mechanism of Protein Transport on the Twin Arginine Translocation Pathway

2018 ◽  
Author(s):  
Steven Theg
Keyword(s):  
Protein Transport ◽  
Twin Arginine Translocation ◽  
Translocation Pathway

A putative twin-arginine translocation pathway in Legionella pneumophila

2004 ◽  
Vol 317 (2) ◽  
pp. 654-661 ◽  
Author(s):  
Emmy De Buck ◽  
Ilya Lebeau ◽  
Liesbeth Maes ◽  
Nick Geukens ◽  
Eef Meyen ◽  
...  
Keyword(s):  
Legionella Pneumophila ◽  
Twin Arginine Translocation ◽  
Translocation Pathway

scholarly journals Functional Analysis of the Twin-Arginine Translocation Pathway inSodalis glossinidius, a Bacterial Symbiont of the Tsetse Fly

2010 ◽  
Vol 77 (3) ◽  
pp. 1132-1134 ◽  
Author(s):  
Linda De Vooght ◽  
Guy Caljon ◽  
Marc Coosemans ◽  
Jan Van Den Abbeele
Keyword(s):  
Escherichia Coli ◽  
Functional Analysis ◽  
Fluorescent Protein ◽  
Bacterial Symbiont ◽  
Tsetse Fly ◽  
Heterologous Proteins ◽  
Twin Arginine Translocation ◽  
Sodalis Glossinidius ◽  
Translocation Pathway ◽  
Green Fluorescent

ABSTRACTThis study demonstrates a functional twin-arginine (Tat) translocation pathway present in the tsetse fly symbiontSodalis glossinidiusand its potential to export active heterologous proteins to the periplasm. Functionality was demonstrated using green fluorescent protein (GFP) fused to the Tat signal peptide ofEscherichia colitrimethylamineN-oxide reductase (TorA).

scholarly journals Stoichiometry for binding and transport by the twin arginine translocation system

2012 ◽  
Vol 197 (4) ◽  
pp. 523-534 ◽  
Author(s):  
Jose M. Celedon ◽  
Kenneth Cline
Keyword(s):  
Kinetic Analysis ◽  
Protein Transport ◽  
Thylakoid Membranes ◽  
Oxygen Evolving Complex ◽  
Receptor Complex ◽  
Twin Arginine Translocation ◽  
Precursor Proteins ◽  
Folded Proteins ◽  
Membrane Components ◽  
Oxygen Evolving

Twin arginine translocation (Tat) systems transport large folded proteins across sealed membranes. Tat systems accomplish this feat with three membrane components organized in two complexes. In thylakoid membranes, cpTatC and Hcf106 comprise a large receptor complex containing an estimated eight cpTatC-Hcf106 pairs. Protein transport occurs when Tha4 joins the receptor complex as an oligomer of uncertain size that is thought to form the protein-conducting structure. Here, binding analyses with intact membranes or purified complexes indicate that each receptor complex could bind eight precursor proteins. Kinetic analysis of translocation showed that each precursor-bound site was independently functional for transport, and, with sufficient Tha4, all sites were concurrently active for transport. Tha4 titration determined that ∼26 Tha4 protomers were required for transport of each OE17 (oxygen-evolving complex subunit of 17 kD) precursor protein. Our results suggest that, when fully saturated with precursor proteins and Tha4, the Tat translocase is an ∼2.2-megadalton complex that can individually transport eight precursor proteins or cooperatively transport multimeric precursors.

scholarly journals Targeting of proteins to the twin‐arginine translocation pathway

2020 ◽  
Vol 113 (5) ◽  
pp. 861-871 ◽  
Author(s):  
Tracy Palmer ◽  
Phillip J. Stansfeld
Keyword(s):  
Twin Arginine Translocation ◽  
Translocation Pathway

scholarly journals The Bacterial Twin-Arginine Translocation Pathway

2006 ◽  
Vol 60 (1) ◽  
pp. 373-395 ◽  
Author(s):  
Philip A. Lee ◽  
Danielle Tullman-Ercek ◽  
George Georgiou
Keyword(s):  
Twin Arginine Translocation ◽  
Translocation Pathway

Novel Twin-Arginine Translocation Pathway-Dependent Phenotypes ofBacillus subtilisUnveiled by Quantitative Proteomics

2013 ◽  
Vol 12 (2) ◽  
pp. 796-807 ◽  
Author(s):  
Vivianne J. Goosens ◽  
Andreas Otto ◽  
Corinna Glasner ◽  
Carmine C. Monteferrante ◽  
René van der Ploeg ◽  
...  
Keyword(s):  
Quantitative Proteomics ◽  
Twin Arginine Translocation ◽  
Translocation Pathway
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