ArticleJournal of bacteriology2010
In Helicobacter pylori, LuxS is a key enzyme in cysteine provision through a reverse transsulfuration pathway.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
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- Effects of Hydrogen Sulfide on the Microbiome: From Toxicity to Therapy.Antioxidants & redox signaling · 2022Review
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- Methionine utilization by bifidobacteria: possible existence of a reverse transsulfuration pathway.Bioscience of microbiota, food and health · 2021Article
- Catalytic specificity of the Lactobacillus plantarum cystathionine γ-lyase presumed by the crystallographic analysis.Scientific reports · 2020Article
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- Potential Role of Biofilm Formation in the Development of Digestive Tract Cancer With Special Reference toFrontiers in microbiology · 2019Article
- Mechanisms of Bacterial Tolerance and Persistence in the Gastrointestinal and Respiratory Environments.Clinical microbiology reviews · 2018Review
- Crystallographic and mutational analyses of cystathionine β-synthase in the HProtein science : a publication of the Protein Society · 2017Article
- The fitness burden imposed by synthesising quorum sensing signals.Scientific reports · 2016Article
- From deep-sea volcanoes to human pathogens: a conserved quorum-sensing signal in Epsilonproteobacteria.The ISME journal · 2015Article
- Biofilm Formation by Helicobacter pylori and Its Involvement for Antibiotic Resistance.BioMed research international · 2015Review
- Integration of untargeted metabolomics with transcriptomics reveals active metabolic pathways.Metabolomics : Official journal of the Metabolomic Society · 2014Article
- Quorum sensing dependent phenotypes and their molecular mechanisms in Campylobacterales.European journal of microbiology & immunology · 2012Review
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7 authors at 3 institutions in 1 country.
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Abstract
In many bacteria, LuxS functions as a quorum-sensing molecule synthase. However, it also has a second, more central metabolic function in the activated methyl cycle (AMC), which generates the S-adenosylmethionine required by methyltransferases and recycles the product via methionine. Helicobacter pylori lacks an enzyme catalyzing homocysteine-to-methionine conversion, rendering the AMC incomplete and thus making any metabolic role of H. pylori LuxS (LuxS(Hp)) unclear. Interestingly, luxS(Hp) is located next to genes annotated as cysK(Hp) and metB(Hp), involved in other bacteria in cysteine and methionine metabolism. We showed that isogenic strains carrying mutations in luxS(Hp), cysK(Hp), and metB(Hp) could not grow without added cysteine (whereas the wild type could), suggesting roles in cysteine synthesis. Growth of the DeltaluxS(Hp) mutant was restored by homocysteine or cystathionine and growth of the DeltacysK(Hp) mutant by cystathionine only. The DeltametB(Hp) mutant had an absolute requirement for cysteine. Metabolite analyses showed that S-ribosylhomocysteine accumulated in the DeltaluxS(Hp) mutant, homocysteine in the DeltacysK(Hp) mutant, and cystathionine in the DeltametB(Hp) mutant. This suggests that S-ribosylhomocysteine is converted by LuxS(Hp) to homocysteine (as in the classic AMC) and thence by CysK(Hp) to cystathionine and by MetB(Hp) to cysteine. In silico analysis suggested that cysK-metB-luxS were acquired by H. pylori from a Gram-positive source. We conclude that cysK-metB-luxS encode the capacity to generate cysteine from products of the incomplete AMC of H. pylori in a process of reverse transsulfuration. We recommend that the misnamed genes cysK(Hp) and metB(Hp) be renamed mccA (methionine-to-cysteine-conversion gene A) and mccB, respectively.
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