Previous work confirmed the role of Hfq and Fur in SodB expression [39]. Deletion of fur results in increased transcription of the sRNAs (rfrA and rfrB) that can pair with mRNA of sodB in an Hfq-dependent fashion and result in the degradation of sodB mRNA. However, a combined deletion of

hfq in Δfur results in loss of rfrAB-mediated degradation of sodB, and results in the synthesis of SodB protein that gets activated to FeSOD in the presence of Fe2+. Our decision to further study ftnB and hmpA was due to our previous findings, where we found that ftnB and hmpA were activated and repressed by Fnr, respectively [21]. The Fnr-dependent expression of ftnB was apparent from the reduced activity in Δfnr under anaerobic conditions, Selleck CX5461 and the reduced activity in the WT strain in presence of oxygen. In addition, iron chelation and the deletion of fur reduced ftnB expression regardless of the oxygen tension. These results indicated that Fur controlled regulation of ftnB is independent of Fnr. Our results are in agreement with earlier work that demonstrated dependence of ftnB expression on Fur [15]. www.selleckchem.com/products/GSK872-GSK2399872A.html However, they are contrary to a previous report, which

determined that Fur exhibited a repressive role on ftnB expression [79]. The reason for this discrepancy is unclear. It is evident from work reported herein and in a previous study in E. coli that ftnB exhibits a strong dependence on low O2 conditions [108]. Furthermore, the earlier study [108] determined that Fnr bound the promoter

of ftnB in E. selleck inhibitor coli and that the Fnr binding site was further upstream than in known Fnr regulated genes. The same investigators [108], postulated that Fnr was unable to induce ftnB and that other regulators were required. However, we have determined that Fnr alone contributes to the activation of ftnB and that Fur is required for full induction of the gene, with Fnr exhibiting a more pronounced role. The lack of a predicted Fur binding site in ftnB indicated that Fur regulation was indirect. The following scenario is proposed to explain these findings and to suggest that the observed regulation of ftnB by Fur is mediated by the histone-like protein H-NS. First, the microarray data showed that Fur negatively regulates the expression of hns and has a predicted Fur binding site (Table 3). Second, we recently demonstrated that Fur binds upstream of hns in a metal dependent fashion [29]. Third, whole genome ChIP analysis demonstrated that H-NS binds to ftnB and the expression of ftnB is up-regulated in the absence of hns [31]. Fourth, the tdc operon is a known target for H-NS repression [31, 76] and was significantly reduced in the absence of fur. Therefore, we propose that the positive regulation ftnB by Fur is mediated by the negative regulation of hns by Fur. Thus removal of Fur (i.e., as in Δfur) results in repression of ftnB by H-NS (see Figure 7).