A common interaction for the entry of colicin N and filamentous phage into Escherichia coli

Hecht, Oliver, Ridley, Helen, Lakey, Jeremy H. and Moore, Geoffrey R. (2009) A common interaction for the entry of colicin N and filamentous phage into Escherichia coli. Journal of Molecular Biology, 388 (4). pp. 880-893. ISSN 0022-2836

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Colicin N is a pore-forming bacteriocin that enters target Escherichia coli cells with the assistance of TolA, a protein in the periplasm of the target cell. The N-terminal domain of the colicin that carries the TolA-binding epitope, the translocation domain (T-domain), is intrinsically disordered. From (1)H-(13)C-(15)N NMR studies of isotopically labeled T-domain interacting with unlabeled TolAIII (the C-terminal domain of TolA), we have identified the TolA-binding epitope and have shown that the extent of its disorder is reduced on binding TolA, although it does not fold into a globular structure with defined secondary structure elements. Residues upstream and downstream of the 27-residue TolA-binding epitope remain disordered in the TolA-bound T-domain as they are in the free T-domain. Filamentous phage also exploits TolAIII to enter target cells, with TolAIII retaining its main secondary structure elements and global fold. In contrast to this, binding of the disordered T-domain of colicin A causes dramatic conformational changes in TolAIII marked by increased flexibility and lack of a rigid tertiary structure consistent with at least partial unfolding of TolAIII, suggesting that bacteriocins and bacteriophages parasitize E. coli using different modes of interaction with TolAIII. We have found that the colicin N T-domain-TolAIII interaction is strikingly similar to the previously described g3p-TolAIII interaction. The fact that both colicin N and filamentous phage exploit TolAIII in a similar manner, with one being a bacterial intrinsically disordered protein and the other being a viral structurally well-ordered protein, suggests that these represent a good example of convergent evolution at the molecular level.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009)
Faculty of Science > School of Chemistry
UEA Research Groups: Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Depositing User: Users 2731 not found.
Date Deposited: 14 Mar 2012 15:13
Last Modified: 23 Oct 2022 01:51
URI: https://ueaeprints.uea.ac.uk/id/eprint/38285
DOI: 10.1016/j.jmb.2009.03.035

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