Related Experiment Video
Updated: Jul 10, 2026

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa
Published on: February 17, 2014
In vitro analysis of the bacterial twin-arginine-dependent protein export
Michael Moser1, Sascha Panahandeh, Eva Holzapfel
1Institut für Biochemie und Molekularbiologie, Zentrum fiir Biochemie und Molekulare Zellforschung, Universität Freiburg, Freiburg, Germany.
Abstract:
Prokaryotic organisms possess a specialized protein translocase in their cytoplasmic membranes that catalyzes the export of folded preproteins. Substrates for this pathway are distinguished by a twin-arginine consensus motif in their signal peptides (twin-arginine translocation [Tat] pathway). We have compiled detailed protocols for the preparation and operation of a cell-free system by which the bacterial Tat pathway can be fully reproduced in vitro. This system has proven useful and is being further exploited for the study of precursor-translocase interactions, assembly of the translocase, and the mechanism of transmembrane passage.
More Related Videos
13:16Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
05:06Characterizing Multidrug Efflux Systems in Acinetobacter baumannii Using an Efflux-Deficient Bacterial Strain and a Single-Copy Gene Expression System
Published on: January 5, 2024
Related Concept Videos
Bacterial Translocation and Protein Secretion
Nuclear Export
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Coordination of Gene Expression Processes in Bacteria