Structural and DNA-binding studies of the PadR-like transcriptional regulator BC1756 from Bacillus cereus

Kim, Tae Hee; Park, Sun Cheol; Lee, Kang-Cheon; Song, Wan Seok; Yoon, Sung‐il

doi:10.1016/j.bbrc.2019.05.141

Cited by 4 publications

(1 citation statement)

References 22 publications

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“…In S. mutans and several other streptococci, lguL (SMU.1603) forms an apparent operon structure with another ORF encoding a putative NAD(P)H-flavin oxidoreductase (SMU.1602) ( Figure 1 ), a conclusion supported by our RT-qPCR (below) and multiple publications of transcriptomic and proteomic analyses that showed co-regulation of these two genes under various conditions [ 29 , 30 ]. Downstream and in opposite orientation to that of SMU.1602–1603 is a putative transcription regulator, SMU.1604c that shares homology with the PadR family repressors [ 31 ]. Adjacent to SMU.1604c and in opposing orientation is SMU.1605, a putative transmembrane protein sharing homology with a drug efflux pump of Bacillus .…”

Section: Resultsmentioning

confidence: 99%

Genetic characterization of glyoxalase pathway in oral streptococci and its contribution to interbacterial competition

Zeng,

Noeparvar,

Burne

et al. 2024

Journal of Oral Microbiology

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Objectives To analyze contributions to microbial ecology of Reactive Electrophile Species (RES), including methylglyoxal, generated during glycolysis. Methods Genetic analyses were performed on the glyoxalase pathway in Streptococcus mutans (SM) and Streptococcus sanguinis (SS), followed by phenotypic assays and transcription analysis. Results Deleting glyoxalase I (lguL) reduced RES tolerance to a far greater extent in SM than in SS, decreasing the competitiveness of SM against SS. Although SM displays a greater RES tolerance than SS, lguL-null mutants of either species showed similar tolerance; a finding consistent with the ability of methylglyoxal to induce the expression of lguL in SM, but not in SS. A novel paralogue of lguL (named gloA2) was identified in most streptococci. SM mutant ∆gloA2SM showed little change in methylglyoxal tolerance yet a significant growth defect and increased autolysis on fructose, a phenotype reversed by the addition of glutathione, or by the deletion of a fructose: phosphotransferase system (PTS) that generates fructose-1-phosphate (F-1-P). Conclusions Fructose contributes to RES generation in a PTS-specific manner, and GloA2 may be required to degrade certain RES derived from F-1-P. This study reveals the critical roles of RES in fitness and interbacterial competition and the effects of PTS in modulating RES metabolism.

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Section: Resultsmentioning

confidence: 99%

Genetic characterization of glyoxalase pathway in oral streptococci and its contribution to interbacterial competition

Zeng,

Noeparvar,

Burne

et al. 2024

Journal of Oral Microbiology

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Apo structure of the transcriptional regulator PadR from Bacillus subtilis: Structural dynamics and conserved Y70 residue

Park

Song

Yoon

2020

Biochemical and Biophysical Research Communications

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Genetic Characterization of Glyoxalase Pathway in Oral Streptococci and its Contribution to Interbacterial Competition

Zeng,

Noeparvar,

Burne

et al. 2023

Preprint

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Substantial quantities of Reactive Electrophile Species (RES), including methylglyoxal and glyoxal, are generated by microbes and humans. To understand the impact of RES on oral microbial homeostasis, genetic analyses were performed on the glyoxalase pathway inStreptococcus mutans(SMU) andStreptococcus sanguinis(SSA). Loss of glyoxalase I (LguL), which catalyzes the rate-limiting reaction in RES degradation, reduced methylglyoxal and glyoxal tolerance to a far greater extent in SMU than in SSA, decreasing the competitiveness of SMU over SSA in planktonic cultures. MICs showed an overall greater RES tolerance by SMU than SSA; a finding consistent with the ability of methylglyoxal to induce the expression oflguLin SMU, but not in SSA. Computational analysis identified a novel paralogue of LguL in most streptococci represented by SMU.1112c in SMU. ΔSMU.1112c showed a minor decrease in methylglyoxal tolerance under certain conditions, but a significant growth defect on fructose; a phenotype reversed by the deletion of a fructose-1-phosphate-generating sugar: phosphotransferase system or addition of glutathione (GSH) to the medium. Further, deletion of the glucose-PTS in SMU increased RES tolerance partly through enhanced expression of the pyruvate-dehydrogenase complex. Consistent with the requirement of GSH for methylglyoxal detoxification, deletion of glutathione synthetase (gshAB) in SMU significantly reduced RES resistance. This study reveals the critical roles of RES in fitness and interbacterial competition and the effects of PTS in modulating RES metabolism. The fact that RES may impact the pathogenic potential of the oral microbiome via differential effects on beneficial and pathogenic species warrants further investigation.

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Structural and DNA-binding studies of the PadR-like transcriptional regulator BC1756 from Bacillus cereus

Cited by 4 publications

References 22 publications

Genetic characterization of glyoxalase pathway in oral streptococci and its contribution to interbacterial competition

Genetic characterization of glyoxalase pathway in oral streptococci and its contribution to interbacterial competition

Apo structure of the transcriptional regulator PadR from Bacillus subtilis: Structural dynamics and conserved Y70 residue

Genetic Characterization of Glyoxalase Pathway in Oral Streptococci and its Contribution to Interbacterial Competition

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