FisR activates σ54 -dependent transcription of sulfide-oxidizing genes in Cupriavidus pinatubonensis JMP134.
Huanjie LiJuan LiChuanjuan LüYongzhen XiaYufeng XinHonglei LiuLuying XunHuaiwei LiuPublished in: Molecular microbiology (2017)
Some heterotrophic bacteria are able to oxidize sulfide (H2 S, HS- and S2- ) 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 σ54 -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 σ54 -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.
Keyphrases
- transcription factor
- genome wide identification
- dna binding
- genome wide
- bioinformatics analysis
- dna methylation
- genome wide analysis
- gene expression
- signaling pathway
- mass spectrometry
- hydrogen peroxide
- copy number
- nitric oxide
- high resolution
- binding protein
- fluorescent probe
- heat shock protein
- heat shock
- liquid chromatography
- solid phase extraction
- heat stress