Identification of genes involved in siderophore transport in Streptomyces coelicolor A3(2)

• Published in: FEMS microbiology letters Vol. 262; no. 1; pp. 57 - 64
• Main Authors: Bunet, Robert, Brock, Anita, Rexer, Hans-Ulrich, Takano, Eriko
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.09.2006; Blackwell; Oxford University Press
• Subjects: ABC transporter; Anti-Bacterial Agents - pharmacology; Antibiotics; Bacterial Proteins - genetics; Bacteriology; Biological and medical sciences; Biological Transport - genetics; Carrier Proteins - genetics; Computational Biology; Deferoxamine - metabolism; Drug Resistance, Bacterial - genetics; fep homologues; Ferric Compounds - metabolism; Ferrichrome - analogs & derivatives; Ferrichrome - pharmacology; Fundamental and applied biological sciences. Psychology; Gene clusters; Gene Deletion; Genes; Genes, Bacterial; Genetics; Genome, Bacterial; Genomes; Iron; Metabolism. Enzymes; Microbiology; Nucleotide sequence; Permeability, membrane transport, intracellular transport; siderophore; Siderophores; Siderophores - metabolism; Streptomyces; Streptomyces coelicolor; Streptomyces coelicolor - genetics; Streptomyces coelicolor - metabolism; Transportation systems; ABC transporter; homologues; siderophore; Streptomycetaceae; Radiolabelling; Streptomyces coelicolor; Escherichia coli; Streptomyces; Identification; Actinomycetales; Gene; Siderophore; Antibiotic resistance; Bacteria; Actinomycetes; fep homologues; Southern blotting; Carrier protein; Enterobacteriaceae
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.2006.00362.x

Abstract The potential iron siderophore transporter genes have been determined from the genome sequence of Streptomyces coelicolor A3(2). One of these gene clusters, cdtABC, was disrupted and characterized to determine its role in the uptake of the siderophores produced by S. coelicolor. Resistance to the siderophore-like antibiotics, salmycin and albomycin, was tested in the parent and cdtABC mutant, showing that the parent, but not the mutant, was sensitive to salmycin, while both were resistant to albomycin. Ferrioxamine competition assays against salmycin suggest that the uptake of salmycin is via a ferrioxamine transport system. However, Fe-55 ferrioxamine B uptake experiments did not reveal any difference between the parent and mutant. This suggests that CdtABC specifically transports salmycin, while ferrioxamine uptake maybe substituted by another transport system.