Publication
Title
An efficient method for the purification of proteins from four distinct toxin-antitoxin modules
Author
Abstract
Toxin-antitoxin (TA) modules are stress response elements that are ubiquitous in the genomes of bacteria and archaea. Production and subsequent purification of individual TA proteins is anything but straightforward as over-expression of the toxin gene is lethal to bacterial and eukaryotic cells and over-production of the antitoxin leads to its proteolytic degradation because of its inherently unstructured nature. Here we describe an effective production and purification strategy centered on an on-column denaturant-induced dissociation of the toxin-antitoxin complex. The success of the method is demonstrated by its application on four different TA families, encoding proteins with distinct activities and folds. A series of biophysical and in vitro activity tests show that the purified proteins are of high quality and suitable for structural studies. (C) 2015 Elsevier Inc. All rights reserved.
Language
English
Source (journal)
Protein expression and purification. - London
Publication
London : 2015
ISSN
1046-5928
Volume/pages
108 (2015) , p. 30-40
ISI
000352176100006
Full text (Publisher's DOI)
Full text (publisher's version - intranet only)
UAntwerpen
Publication type
Subject
External links
Web of Science
Record
Identification
Creation 04.10.2018
Last edited 25.08.2021