Journal of Bacteriology, August 2008, p. 5143-5152, Vol. 190, No. 15
0021-9193/08/$08.00+0 doi:10.1128/JB.00464-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Fachbereich Chemie/Biochemie der Philipps-Universität Marburg, Hans Meerwein Strasse, D-35032 Marburg, Germany,1 Lehrstuhl für Biologische Chemie, Technische Universität München, Freising-Weihenstephan, Germany2
Received 4 April 2008/ Accepted 16 May 2008
High-affinity iron acquisition in Bacillus subtilis is mediated via the bacillibactin catechole siderophore pathway. Three of the four essential pathway steps, bacillibactin synthesis, Fe-bacillibactin uptake, and Fe-bacillibactin hydrolysis have been characterized previously. The functional and regulatory components for bacillibactin secretion, the second step of the siderophore pathway, remained unknown. In this study, the screening of a B. subtilis exporter mutant library led to the identification of the YmfE major facilitator superfamily (MFS)-type transporter as a target for bacillibactin export. Analysis of iron-limited ymfE mutant cultures displayed an eightfold reduced bacillibactin secretion and, on the other hand, a 25-fold increased secretion of the bacillibactin precursor 2,3-dihydroxybenzoate. Investigation of the regulatory aspect revealed that bacillibactin secretion is, in contrast to all other components of the pathway, independent of the ferric uptake repressor Fur. Indeed, the MerR-type transcriptional regulator Mta was found to activate both bacillibactin secretion and ymfE gene expression, exposing Mta as an additional regulatory member of the bacillibactin pathway.
Published ahead of print on 23 May 2008.
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