Toggle Main Menu Toggle Search

Open Access padlockePrints

The Newcastle University research output collection, currently available on ePrints, will shortly be moving to a new open repository platform, Figshare. To prepare for the data migration we have paused adding new content to ePrints, and will resume once the new repository is launched. During this time you will continue to have access to ePrints (but no new content will appear). We will share updates here when available.

Bacterial toxin colicin N-T domain structure changes to ordered state upon binding C-terminal domain of TolA

Lookup NU author(s): Dr Yakup Ulusu, Emeritus Professor Jeremy LakeyORCiD, Isa Gokce

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

Colicin N is a bacterial toxin that kills Escherichia coli and related cells. Its mode of action is of interest in protein import and toxicology. Colicin N translocates across the E. coli outer membrane and periplasm by interacting with several receptors. The translocation process involves the interaction of the colicin N with the outer membrane porin OmpF and subsequently with the integral membrane protein TolA. The N-terminal domain of colicin N is involved in the import process. TolA consists of 3 domains. The N-terminal domain of colicin N interacts with the C-terminal domain of TolA at later stages of the translocation process. Our aim was to produce a large quantity of colicin N T-domains for spectroscopic and crystallization studies. These both require a correctly folded and stable protein. Here we present an expression of the complex between the N-terminal domain of colicin N and the C-terminal domain of TolA obtained by fusing these 2 domains with a flexible linker. Circular dichroism spectroscopy studies indicated that unstructured bacterial toxin colicin N T-domains changed to an ordered state upon binding to the C-terminal domain of TolA; this fusion protein has a secondary and tertiary structure.

Publication metadata

Author(s): Ulusu Y, Senturk SB, Gedikli F, Lakey JH, Gokce I

Publication type: Article

Publication status: Published

Journal: Turkish Journal of Biology

Year: 2014

Volume: 38

Issue: 5

Pages: 648-652

Print publication date: 30/09/2014

Online publication date: 05/09/2014

Acceptance date: 03/06/2014

ISSN (print): 1300-0152

ISSN (electronic): 1303-6092

Publisher: TUBITAK: Scientific & Technical Research Council, Turkey

URL: http://dx.doi.org/10.3906/biy-1401-30

DOI: 10.3906/biy-1401-30

Altmetrics

Altmetrics provided by Altmetric

Share