期刊
MOLECULAR MICROBIOLOGY
卷 105, 期 3, 页码 373-384出版社
WILEY
DOI: 10.1111/mmi.13725
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资金
- National Natural Science Foundation of China [21477062, 31500047]
- National Key Research and Development Program of China [2016YFA0601103]
- Natural Science foundation of Shandong Province [ZR2014CM003, ZR2016CM03]
- Fundamental Research Funds of Shandong University [11200075614013]
- State Key Laboratory of Microbial Technology at Shandong University
Some heterotrophic bacteria are able to oxidize sulfide (H2S, HS- and S-2(-)) to sulfite and thiosulfate via polysulfide. The genes coding for the oxidation enzymes in Cupriavidus pinatubonensis JMP134 have recently been identified; however, their regulation is unknown. A regulator gene is adjacent to the operon of the sulfide-oxidizing genes, encoding a sigma(54)-dependent transcription factor (FisR) with three domains: an R domain, an AAA+ domain and a DNA-binding domain. Here it is reported that the regulator responds to the presence of sulfide and activates the sulfide-oxidizing genes. FisR binds to its cognate operator at -114 to -135 bp of the transcription start of the operon. When polysulfide reacts with the R domain of FisR through the three conserved cysteine residues (C53, C64 and C71), FisR activates the expression of the operon. FisR is highly sensitive to polysulfide, activating sigma(54)-dependent transcription of sulfide-oxidizing genes for sulfide removal. Further, sequence analysis indicates that FisR-type regulators are relatively common for controlling sulfide-oxidizing genes under sulfide stress in the Proteobacteria.
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