Generation of hydrogen sulfide from sulfur assimilation in <i>Escherichia coli</i>

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  • Tanaka Naoyuki
    Gradutate of School of Life and Environmental Sciences, University of Tsukuba
  • Hatano Tomoyuki
    Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of Warwick
  • Saito Soshi
    Technical Research Laboratories, Kyowa Hakko Bio, Ltd.
  • Wakabayashi Yukari
    Technical Research Laboratories, Kyowa Hakko Bio, Ltd.
  • Abe Tetsuya
    Technical Research Laboratories, Kyowa Hakko Bio, Ltd.
  • Kawano Yusuke
    Gradutate of School of Life and Environmental Sciences, University of Tsukuba
  • Ohtsu Iwao
    Gradutate of School of Life and Environmental Sciences, University of Tsukuba

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<p>Many organisms produce endogenous hydrogen sulfide (H2S) as a by-product of protein, peptide, or L-cysteine degradation. Recent reports concerning mammalian cells have demonstrated that H2S acts as a signaling molecule playing important roles in various biological processes. In contrast to mammals, bacterial H2S signaling remains unclear. In this work, we demonstrate that Escherichia coli generates H2S through the assimilation of inorganic sulfur, without L-cysteine degradation. Comparison of phenotypes and genomes between laboratory E. coli K-12 strains revealed a major contribution of CRP (a protein that controls the expression of numerous genes involved in glycolysis) to H2S generation. We found that H2S was produced by cells growing in a synthetic minimal medium containing thiosulfate as a sole inorganic sulfur source, but not in a medium only containing sulfate. Furthermore, E. coli generated H2S in a CRP-dependent manner as a response to glucose starvation. These results indicate that CRP plays a key role in the generation of H2S coupled to thiosulfate assimilation, whose molecular mechanisms remains to be elucidated. Here, we propose a potential biological role of the H2S as a signaling mediator for a cross-talk between carbon and sulfur metabolism in E. coli.</p>

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