{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zeng L"],"funding":["NIDCR NIH HHS","National Institute of Dental and Craniofacial Research"],"pagination":["2322241"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10911100"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["<h4>Objectives</h4>To analyze contributions to microbial ecology of Reactive Electrophile Species (RES), including methylglyoxal, generated during glycolysis.<h4>Methods</h4>Genetic analyses were performed on the glyoxalase pathway in Streptococcus mutans (SM) and Streptococcus sanguinis (SS), followed by phenotypic assays and transcription analysis.<h4>Results</h4>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).<h4>Conclusions</h4>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."],"journal":["Journal of oral microbiology"],"pubmed_title":["Genetic characterization of glyoxalase pathway in oral streptococci and its contribution to interbacterial competition."],"pmcid":["PMC10911100"],"funding_grant_id":["DE012236","R01 DE012236"],"pubmed_authors":["Noeparvar P","Burne RA","Zeng L","Glezer BS"],"additional_accession":[]},"is_claimable":false,"name":"Genetic characterization of glyoxalase pathway in oral streptococci and its contribution to interbacterial competition.","description":"<h4>Objectives</h4>To analyze contributions to microbial ecology of Reactive Electrophile Species (RES), including methylglyoxal, generated during glycolysis.<h4>Methods</h4>Genetic analyses were performed on the glyoxalase pathway in Streptococcus mutans (SM) and Streptococcus sanguinis (SS), followed by phenotypic assays and transcription analysis.<h4>Results</h4>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).<h4>Conclusions</h4>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.","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-06-14T05:37:53.196Z","creation":"2025-04-06T17:17:04.816Z"},"accession":"S-EPMC10911100","cross_references":{"pubmed":["38440286"],"doi":["10.1080/20002297.2024.2322241"]}}