Toggle Main Menu Toggle Search

Open Access padlockePrints

Self-recognition by an intrinsically disordered protein

Lookup NU author(s): Dr David Allen Chalton, Professor Jeremy LakeyORCiD

Downloads

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


Abstract

The intrinsically disordered translocation domain (T-domain) of the protein antibiotic colicin N binds to periplasmic receptors of target Escherichia coli cells in order to penetrate their inner membranes. We report here that the specific 27 consecutive residues of the T-domain of colicin N known to bind to the helper protein TolA in target cells also interacts intramolecularly with folded regions of colicin N. We suggest that this specific self-recognition helps intrinsically disordered domains to bury their hydrophobic recognition motifs and protect them against degradation, showing that an impaired self-recognition leads to increased protease susceptibility. © 2008 Federation of European Biochemical Societies.


Publication metadata

Author(s): Hecht O, Ridley H, Boetzel R, Lewin A, Cull N, Chalton DA, Lakey JH, Moore GR

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2008

Volume: 582

Issue: 17

Pages: 2673-2677

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: Elsevier BV

URL: http://dx.doi.org/10.1016/j.febslet.2008.06.022

DOI: 10.1016/j.febslet.2008.06.022


Altmetrics

Altmetrics provided by Altmetric


Funding

Funder referenceFunder name
British Heart Foundation
082045Wellcome Trust
40422Wellcome Trust
66850Wellcome Trust
BB/F005768/1Biotechnology and Biological Sciences Research Council
55979Wellcome Trust
56232Wellcome Trust
BB/C507396/1Biotechnology and Biological Sciences Research Council
bb/c507402Wellcome Trust
MC_U117533887Medical Research Council

Share