Characterisation of the interaction of colicin A with its co-receptor TolA

Hecht, Oliver; Zhang, Ying; Li, Chan; Penfold, Christopher N.; James, Richard; Moore, Geoffrey R.

doi:10.1016/j.febslet.2010.04.061

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Volume 584, Issue 11 , Pages 2249-2252, 3 June 2010

Characterisation of the interaction of colicin A with its co-receptor TolA

Edited by Stuart Ferguson

Oliver Hecht
- Centre for Molecular and Structural Biochemistry School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, UK
Ying Zhang
- Centre for Biomolecular Sciences, School of Molecular Medical Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK
Chan Li
- Centre for Biomolecular Sciences, School of Molecular Medical Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK
Christopher N. Penfold
- Centre for Biomolecular Sciences, School of Molecular Medical Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK
Richard James
- Centre for Biomolecular Sciences, School of Molecular Medical Sciences, University Park, University of Nottingham, Nottingham NG7 2RD, UK
Geoffrey R. Moore
- Centre for Molecular and Structural Biochemistry School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, UK
- Corresponding author. Fax: +44 1603 592003.

Received 12 February 2010; received in revised form 16 April 2010; accepted 19 April 2010. published online 28 April 2010.

Abstract

Colicin A enters Escherichia coli cells through interaction with endogenous TolA and TolB proteins. In vitro, binding of the colicin A translocation domain to TolA leads to unfolding of TolA. Through NMR studies of the colicin A translocation domain and polypeptides representing the individual TolA and TolB binding epitopes of colicin A we question if the unfolding of TolA induced by colicin A is likely to be physiologically relevant. The NMR data further reveals that the colicin A binding site on TolA is different from that for colicin N which explains why there is a difference in colicin toxicity for E. coli carrying a TolA-III homologue from Yersina enterocolitica in place of its own TolA-III.

Structured summary

MINT-7888512: TolA (uniprotkb:P19934) and Col-A (uniprotkb:P04480) bind (MI:0407) by nuclear magnetic resonance (MI:0077)

MINT-7888526: TolA (uniprotkb:P19934) and TolB (uniprotkb:P0A857) bind (MI:0407) by nuclear magnetic resonance (MI:0077)

MINT-7888999: TolA (uniprotkb:P19934), TolB (uniprotkb:P0A855) and Col-A (uniprotkb:P04480) physically interact (MI:0915) by molecular sieving (MI:0071)

MINT-7888982: TolA (uniprotkb:P19934), TolB (uniprotkb:P0A855) and Col-A (uniprotkb:P04480) physically interact (MI:0915) by nuclear magnetic resonance (MI:0077)

Keywords: Intrinsically disordered protein, Colicin A, TolA, NMR, Protein–protein interaction