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Fig. 5 | Microbial Cell Factories

Fig. 5

From: OhsR acts as an organic peroxide-sensing transcriptional activator using an S-mycothiolation mechanism in Corynebacterium glutamicum

Fig. 5

Induction of the expression of OhsR by CHP. Cells were grown in LB medium to an OD600 nm of 0.6. OhsR expression was analyzed after indicated CHP addition. a β-Galactosidase analyses of ohsR promoter activities by using the transcriptional PohsR::lacZ chromosomal fusion reporter expressed in indicated strains under stress conditions. b Quantitative RT-PCR analyses of ohsR expression in indicated strains exposed to stress conditions for 4.5 h. Results were the average of four independent experiments; the standard deviation is indicated by bars. **P < 0.01; *P ≤ 0.05. n.s. not significant. c The protein levels of OhsR in wild type with or without peroxides treatment. Lysates from bacteria exposed to stress conditions for 4.5 h were resolved by SDS-PAGE, and OhsR was detected by immunoblotting using specific anti-OhsR antibody. For the pellet fraction, RNA polβ was used as a loading control. Similar results were obtained in three independent experiments, and data shown are from one representative experiment done in triplicate (Left panel). Relative quantified data for protein levels by Image Lab (Right panel). Quantified protein expression of western blots in c. Densities of proteins were all justified with α-RNA polβ. Relative density ratios of wild-type without stress were set at a value of 1.0. Data shown were the averages of three independent experiments, and error bars indicate the SDs from three independent experiments. **P < 0.01; *P < 0.05. n.s. not significant

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