Our data showed that the mioC mutant is defective in both biofilm

Our data showed that the mioC mutant is defective in both biofilm formation and aggregation, Doxorubicin molecular weight which suggested that the mioC gene may be important for biofilm formation in P. aeruginosa, which is consistent with other reports. Interestingly, biofilm formation of the mioC mutant was boosted under iron depletion and some metal stresses. Fld has been shown to replace bacterial ferredoxin

and this protein can enhance bacterial tolerance to iron starvation (Sancho, 2006). Therefore, the mioC gene mutant may feel stressed under iron depletion so that more biofilms are produced for their survival under this condition. Also, metals are known to induce oxidative stress in bacterial cell and bacterial Fld influences in the defense against oxidative stress (Imlay, 2006; Sancho, 2006). Thus, the mioC mutant is in danger under excess metal conditions and induces

biofilm formation as a defense. It has been shown that motility is important for E. coli and P. aeruginosa biofilm formation (O’Toole & Kolter, 1998; Pratt & Kolter, 1999). Consistent with those data, we demonstrated that motility and biofilm formation were enhanced in the mioC mutant under iron-depleted conditions. Pyocyanin has been reported to function as an electron shuttle for iron acquisition (Hernandez et al., 2004). Natural products such as pyocyanin may promote microbial metal reduction in the environment (Hernandez et al., 2004). In addition, pyocyanin alters the carbon flux of carbon metabolism (Price-Whelan drug discovery et al., 2007). Dichloromethane dehalogenase In this study, we suggested that the mioC mutant strain may be very sensitive to iron limitation, over-producing pyocyanin in response. The mutant cells were also sensitive to metal stresses. Therefore, the mioC mutant cell may

recognize the deficiency of the reduced metal due to depletion of Fld, which functions as an electron donor in bacteria, and therefore produces pyocyanin to acquire metals from the environment. Interestingly, cell death after the stationary phase was accelerated in the mioC mutant cell, whereas there was no difference in exponential growth rate between the cells (wild type, 0.43 ± 0.04; ∆mioC, 0.41 ± 0.03; mioC OE, 0.41 ± 0.05) (Fig. S5). This means that pyocyanin-induced over-production of mutant may be able to promote cell death with redox imbalance, because pyocyanin generates reactive oxygen species that induce oxidative stress in bacteria (Hassan & Fridovich, 1980). It has been proposed that the long-chain Flds may have preceded the shorter ones, such as MioC (Sancho, 2006). Interestingly, Fld is not present in higher eukaryotes and appears fused in multi-domain proteins of eukaryotes. Escherichia coli has some Fld in its genome; however, one Fld (MioC) is annotated in the Pseudomonas species chromosomes (Yeom et al., 2009a). Therefore, Pseudomonas species may be closer from an evolutionary perspective to eukaryotes than E.

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