Lookup NU author(s): Dr David Allen Chalton,
Professor Jeremy Lakey
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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.
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
ISSN (print): 0014-5793
ISSN (electronic): 1873-3468
Publisher: Elsevier BV
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