ferrichrome-a and rhodotorulic-acid

To assess which types of siderophores are typically produced by Brevibacterium and how siderophore production and utilization traits are distributed within this genus.. During co-cultivation experiments it was found that growth of B. linens Br5 was stimulated by B. linens NIZO B1410 by two orders of magnitude. The stimulation was caused by the production of hydroxamate siderophores by B. linens NIZO B1410 that enabled the siderophore-auxotrophic strain Br5 to grow faster under the applied iron-limited growth conditions. Different patterns of siderophore production and utilization were observed within the genus Brevibacterium. These patterns did not reflect the phylogenetic relations within the group as determined by partial 16S rDNA sequencing. Most Brevibacterium strains were found to utilize hydroxamate siderophores.. Brevibacteria can produce and utilize siderophores although certain strains within this genus are siderophore-auxotrophic.. It is reported for the first time that brevibacteria produce and utilize siderophores. This knowledge can be utilized to stimulate growth of auxotrophic strains under certain conditions. Enhancing the growth rate of Brevibacterium is of importance for the application of this species, for example, for cheese manufacturing or for industrial production of enzymes or metabolites.

Topics: Bacteriological Techniques; Brevibacterium; Catechols; Culture Media; Deferoxamine; DNA, Bacterial; DNA, Ribosomal; Ethylenediamines; Ferric Compounds; Ferrichrome; Food Microbiology; Hydroxybenzoates; Iron; Iron Chelating Agents; Phylogeny; Piperazines; Siderophores

A family of four putative transporters (Arn1p-4p) in Saccharomyces cerevisiae is expressed under conditions of iron deprivation and is regulated by Aft1p, the major iron-dependent transcription factor in yeast. One of these, Arn3p/Sit1p, facilitates the uptake of ferrioxamine B, a siderophore of the hydroxamate class. Here we report that ARN family members facilitated the uptake of iron from the trihydroxamate siderophores ferrichrome, ferrichrome A, and triacetylfusarinine C. Uptake of siderophore-bound iron was dependent on either the high-affinity ferrous iron transport system or the ARN family of transporters. The specificity of each siderophore for individual transporters was determined. Uptake of ferrichrome and ferrichrome A was facilitated by both Arn1p and Arn3p. Uptake of triacetylfusarinine C was facilitated by Arn2p, although small amounts of uptake also occurred through Arn1p and Arn3p. In contrast to the trihydroxamates, uptake of iron from the dihydroxamate rhodotorulic acid occurred only via the high-affinity ferrous iron system. Epitope-tagged Arn1p was expressed in intracellular vesicles in a pattern that was indistinguishable from that of Arn3p, whereas Ftr1p, a component of the high-affinity ferrous system, was expressed on the plasma membrane. These data indicate that S. cerevisiae maintains two systems of siderophore uptake, only one of which is located on the plasma membrane.

Topics: Biological Transport; Carrier Proteins; Cell Membrane; Ceruloplasmin; Ferric Compounds; Ferrichrome; Fluorescent Antibody Technique; FMN Reductase; Hydroxamic Acids; Iron; Kinetics; Membrane Proteins; Membrane Transport Proteins; Mutation; NADH, NADPH Oxidoreductases; Piperazines; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Siderophores