Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp

Grinter, R., Milner, J. and Walker, D. (2012) Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp. PLoS ONE, 7(3), e33033. (doi: 10.1371/journal.pone.0033033) (PMID:22427936) (PMCID:PMC3302902)

[img] Text
Available under License Creative Commons Attribution.



In order to kill competing strains of the same or closely related bacterial species, many bacteria produce potent narrow-spectrum protein antibiotics known as bacteriocins. Two sequenced strains of the phytopathogenic bacterium <i>Pectobacterium carotovorum</i> carry genes encoding putative bacteriocins which have seemingly evolved through a recombination event to encode proteins containing an N-terminal domain with extensive similarity to a [2Fe-2S] plant ferredoxin and a C-terminal colicin M-like catalytic domain. In this work, we show that these genes encode active bacteriocins, pectocin M1 and M2, which target strains of <i>Pectobacterium carotovorum</i> and <i>Pectobacterium atrosepticum</i> with increased potency under iron limiting conditions. The activity of pectocin M1 and M2 can be inhibited by the addition of spinach ferredoxin, indicating that the ferredoxin domain of these proteins acts as a receptor binding domain. This effect is not observed with the mammalian ferredoxin protein adrenodoxin, indicating that <i>Pectobacterium spp.</i> carries a specific receptor for plant ferredoxins and that these plant pathogens may acquire iron from the host through the uptake of ferredoxin. In further support of this hypothesis we show that the growth of strains of <i>Pectobacterium carotovorum</i> and <i>atrosepticum</i> that are not sensitive to the cytotoxic effects of pectocin M1 is enhanced in the presence of pectocin M1 and M2 under iron limiting conditions. A similar growth enhancement under iron limiting conditions is observed with spinach ferrodoxin, but not with adrenodoxin. Our data indicate that pectocin M1 and M2 have evolved to parasitise an existing iron uptake pathway by using a ferredoxin-containing receptor binding domain as a Trojan horse to gain entry into susceptible cells.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Walker, Professor Daniel and Milner, Dr Joel and Grinter, Mr Rhys
Authors: Grinter, R., Milner, J., and Walker, D.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
College of Medical Veterinary and Life Sciences > School of Life Sciences
Journal Name:PLoS ONE
Publisher:Public Library of Science
ISSN (Online):1932-6203
Published Online:09 March 2012
Copyright Holders:Copyright © 2012 The Authors
First Published:First published in PLoS ONE 7(3):e33033
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

University Staff: Request a correction | Enlighten Editors: Update this record