The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore
S I Patzer1, M R Baquero2, D Bravo2
1Mikrobiologie/Membranphysiologie, Universität Tübingen, Auf der Morgenstelle 28, Tübingen, Germany.
Abstract:
The colicin G producer Escherichia coli CA46, the colicin H producer E. coli CA58 and E. coli Nissle 1917 (DSM 6601) were shown to produce microcin H47 and the newly described microcin M. Both microcins were exported like colicin V by an RND-type export system, including TolC. The gene cluster encoding microcins H47 and M in strains CA46 and CA58 is nearly identical to that in strain DSM 6601, except that two additional genes are included. A Fur box identified in front of the microcin-encoding genes explained the observed iron regulation of microcin production. The catecholate siderophore receptors Fiu, Cir and FepA from E. coli and IroN, Cir and FepA from Salmonella were identified as receptors for microcins M, H47 and E492. IroN takes up the glucose-containing catecholate siderophore salmochelin, whose synthesis is encoded in the iro gene cluster found in Salmonella and certain, often uropathogenic, E. coli strains. A gene in this iro cluster, iroB, which encodes a putative glycosyltransferase, was also found in the microcin H47/M and microcin E492 gene clusters. These microcins could aid the producing strain in competing against enterobacteria that utilize catecholate siderophores.
Insights
Escherichia coli produces microcins H47 and M, utilizing RND-type export systems and specific receptors for iron uptake. These microcins enhance competitive advantages against other enterobacteria.
Area of Science:
- Microbiology
- Bacteriology
- Molecular Biology
Background:
- Escherichia coli strains produce various colicins and microcins, which are proteinaceous toxins involved in interbacterial competition.
- The export mechanisms and receptor interactions of these bacteriocins are crucial for their function and host range.
Purpose of the Study:
- To characterize the production, export, and receptor usage of newly identified microcins H47 and M from Escherichia coli.
- To elucidate the genetic basis and regulation of microcin H47 and M production.
Main Methods:
- Comparative genomic analysis of microcin gene clusters.
- Identification of export systems and outer membrane receptors through genetic and biochemical approaches.
- Investigation of iron-dependent regulation using Fur box analysis.
Main Results:
- Escherichia coli strains CA46, CA58, and Nissle 1917 produce microcins H47 and M, exported via an RND-type system including TolC.
- The gene clusters for microcins H47 and M share significant homology, with variations in gene content.
- Iron regulation of microcin production is mediated by a Fur box.
- Catecholate siderophore receptors (Fiu, Cir, FepA, IroN) were identified as receptors for microcins M, H47, and E492.
- The iroB gene, involved in salmochelin synthesis, is present in microcin gene clusters.
Conclusions:
- Microcins H47 and M are exported through a TolC-dependent RND system.
- The presence of the iroB gene suggests a link between microcin production and catecholate siderophore utilization.
- These microcins likely confer a competitive advantage to producing strains against enterobacteria employing catecholate siderophores.
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