Journal
SCIENTIFIC REPORTS
Volume 12, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41598-022-09237-2
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Funding
- Fundacio La Marato de TV3 [201815]
- [PID2019-107725RG-I00]
- [2017SGR3]
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Bacillus subtilis is a bacterium found in the human microbiome that can infect immunocompromised patients. It has a transposon called ICEBs1, which can be transferred to other bacteria, including pathogenic Bacillus anthracis and Listeria monocytogenes. This study focuses on the regulation of ICEBs1 by ImmR/ImmA and the crystal structure of ImmR's DNA-binding domain, revealing its potential role in binding to target DNA.
Bacillus subtilis is a commensal member of the human oral and gut microbiomes, which can become infectious to immunocompromised patients. It possesses a conjugative transposon, ICEBs1, which includes > 20 genes and can be passed by horizontal gene transfer to other bacteria, including pathogenic Bacillus anthracis and Listeria monocytogenes. ICEBs1 is regulated by the ImmR/ImmA tandem, which are a transcriptional repressor that constitutively blocks transcription and a metallopeptidase that acts as anti-repressor and inactivates ImmR by proteolytic cleavage. We here report the production and purification of 127-residue ImmR from ICEBs1 and the crystal structure of its DNA-binding domain. It features a five-helix bundle centred on a helix-turn-helix motif potentially binding the major grove of double-stranded target DNA. ImmR shows structural and mechanistic similarity with the B. subtilis SinR repressor, which is engaged in sporulation inhibition.
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