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Self-recognition by an intrinsically disordered protein

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


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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


DOI: 10.1016/j.febslet.2008.06.022


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