Campylobacter
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA600010 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR15054000_1.fastq.gz | Fastqsanger.gz | |||
| SRR15054000_2.fastq.gz | Fastqsanger.gz | |||
| SRR15054100_1.fastq.gz | Fastqsanger.gz | |||
| SRR15054100_2.fastq.gz | Fastqsanger.gz | |||
| SRR15054200_1.fastq.gz | Fastqsanger.gz |
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Project description:The pathogenic bacterium Campylobacter jejuni is the leading cause of bacterial foodborne gastroenteritis worldwide yet it does not grow in the aerobic environment. The paralogues RrpA and RrpB which are members of MarR family of DNA binding proteins have been shown to be important for the survival of C. jejuni under aerobic and redox stress. We report that RrpA is a positive regulator of mdaB, encoding a flavin-dependent quinone reductase. MdaB confers protection to the cell from redox stress mediated by structurally diverse quinones. RrpB negatively regulates the expression of nfrA (Cj1555c), a flavin reductase. NfrA reduces riboflavin at a much higher rate than flavin mononucleotide (FMN),suggesting exogenous free flavins are the natural substrate. Enzymatic activity of MdaB and NfrA towards their substrates revealed both reductases preferred NADPH as an electron donor. DNA-binding and post translational modification analyses showed that the mechanism of RrpA and RrpB DNA binding is likely a cysteine-based redox switch. Complete genome sequences analysis indicated that MdaB is predominant in Campylobacter spp. and the related Helicobacter spp., whilst NfrA is more often found in C. jejuni strains. Quinones and flavins are antimicrobial redox cycling agents secreted by a wide range of cell-types that can form damaging superoxide by one-electron reactions. We propose that MdaB and NfrA production allows a two-electron reduction mechanism to the less toxic quinol forms. These enzymes thus aid the survival and persistence of C. jejuni in the face of toxic compounds from competing microbes.
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