ArticlePloS one2012
Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Antibacterial and antibiofilm activities of pyocins produced byFrontiers in microbiology · 2026Pooled it
- The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.Journal of structural biology: X · 2025Article
- Pyocins and Beyond: Exploring the World of Bacteriocins in Pseudomonas aeruginosa.Probiotics and antimicrobial proteins · 2025Review
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.FEBS open bio · 2024Article
- Impact of Homologous Recombination on Core Genome Evolution and Host Adaptation of Pectobacterium parmentieri.Genome biology and evolution · 2024Article
- Engineering ofCells · 2023Article
- Unleashing the Influence of cAMP Receptor Protein: The Master Switch of Bacteriocin Export inInternational journal of molecular sciences · 2023Article
- The Evolutionary History of Peptidases Involved in the Processing of Organelle-Targeting Peptides.Genome biology and evolution · 2022Article
- Unraveling the Uncharacterized Domain of Carocin S2: A RibonucleaseMicroorganisms · 2022Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- Anticancer and antimicrobial potential of enterocin 12a from Enterococcus faecium.BMC microbiology · 2021Article
- CbrA Mediates Colicin M Resistance in Escherichia coli through Modification of Undecaprenyl-Phosphate-Linked Peptidoglycan Precursors.Journal of bacteriology · 2020Article
- Article
- The crystal structure of the TonB-dependent transporter YncD reveals a positively charged substrate-binding site.Acta crystallographica. Section D, Structural biology · 2020Article
- Engineering bacteriocin-mediated resistance against the plant pathogen Pseudomonas syringae.Plant biotechnology journal · 2020Article
- Bacteriocins Targeting Gram-Negative Phytopathogenic Bacteria: Plantibiotics of the Future.Frontiers in microbiology · 2020Review
- Genome-Wide Analyses Revealed Remarkable Heterogeneity in Pathogenicity Determinants, Antimicrobial Compounds, and CRISPR-Cas Systems of Complex Phytopathogenic GenusPathogens (Basel, Switzerland) · 2019Article
- Protease-associated import systems are widespread in Gram-negative bacteria.PLoS genetics · 2019Article
- Draft Genome Sequence of the Necrotrophic Plant-Pathogenic Bacterium Pectobacterium carotovorum subsp. carotovorum Strain LMG 2410.Microbiology resource announcements · 2019Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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