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A Natively Unfolded Toxin Domain Uses Its Receptor as a Folding Template

Lookup NU author(s): Professor Jeremy LakeyORCiD


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Natively unfolded proteins range from molten globules to disordered coils. They are abundant in eukaryotic genomes and commonly involved in molecular interactions. The essential N-terminal translocation domains of colicin toxins from Escherichia coli are disordered bacterial proteins that bind at least one protein of the Tol or Ton family. The colicin N translocation domain (ColN-(1-90)), which binds to the C-terminal domain of TolA (TolA-(296-421)), shows a disordered far-UV CD spectrum, no near-UV CD signal, and non-cooperative thermal unfolding. As expected, TolA-(296-421) displays both secondary structure in far-UV CD and tertiary structure in near-UV CD. Furthermore it shows a cooperative unfolding transition at 65°C. CD spectra of the 1:1 complex show both increased secondary structure and colicin N-specific near-UV CD signals. A new cooperative thermal transition at 35°C is followed by the unchanged unfolding behavior of TolA-(296-421). Fluorescence and surface plasmon resonance confirm that the new unfolding transition accompanies dissociation of ColN-(1-90). Hence upon binding the disordered structure of ColN-(1-90) converts to a cooperatively folded domain without altering the TolA-(296-421) structure.

Publication metadata

Author(s): Anderluh G, Gokce I, Lakey JH

Publication type: Article

Publication status: Published

Journal: Journal of Biological Chemistry

Year: 2004

Volume: 279

Issue: 21

Pages: 22002-22009

Print publication date: 21/05/2004

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: The American Society for Biochemistry and Molecular Biology, Inc


DOI: 10.1074/jbc.M313603200

PubMed id: 15004032


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