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

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 Pectobacterium carotovorum carry genes encoding putative bacteriocins wh...

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Autores principales: Rhys Grinter, Joel Milner, Daniel Walker
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Publicado: Public Library of Science (PLoS) 2012
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spelling oai:doaj.org-article:e544f8bb7f2642698f6f8346eea2c9702021-11-18T07:25:37ZFerredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.1932-620310.1371/journal.pone.0033033https://doaj.org/article/e544f8bb7f2642698f6f8346eea2c9702012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22427936/?tool=EBIhttps://doaj.org/toc/1932-6203In 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 Pectobacterium carotovorum 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 Pectobacterium carotovorum and Pectobacterium atrosepticum 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 Pectobacterium spp. 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 Pectobacterium carotovorum and atrosepticum 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.Rhys GrinterJoel MilnerDaniel WalkerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 3, p e33033 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Rhys Grinter
Joel Milner
Daniel Walker
Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
description 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 Pectobacterium carotovorum 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 Pectobacterium carotovorum and Pectobacterium atrosepticum 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 Pectobacterium spp. 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 Pectobacterium carotovorum and atrosepticum 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.
format article
author Rhys Grinter
Joel Milner
Daniel Walker
author_facet Rhys Grinter
Joel Milner
Daniel Walker
author_sort Rhys Grinter
title Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
title_short Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
title_full Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
title_fullStr Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
title_full_unstemmed Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
title_sort ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in pectobacterium spp.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/e544f8bb7f2642698f6f8346eea2c970
work_keys_str_mv AT rhysgrinter ferredoxincontainingbacteriocinssuggestanovelmechanismofironuptakeinpectobacteriumspp
AT joelmilner ferredoxincontainingbacteriocinssuggestanovelmechanismofironuptakeinpectobacteriumspp
AT danielwalker ferredoxincontainingbacteriocinssuggestanovelmechanismofironuptakeinpectobacteriumspp
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