Chromate is a widespread pollutant as a waste of human activities. However, the mechanisms underlying its high toxicity are not clearly understood. In this work, we used the yeast Saccharomyces cerevisiae to analyse the physiological effects of chromate exposure in a eukaryote cell model. We show that chromate causes a strong decrease of sulfate assimilation and sulfur metabolite pools suggesting that cells experience sulfur starvation. As a consequence, nearly all enzymes of the sulfur pathway are highly induced as well as enzymes of the sulfur-sparing response such as Pdc6, the sulfur-poor pyruvate decarboxylase. The induction of Pdc6 was regulated at the mRNA level and dependent upon Met32, a coactivator of Met4, the transcriptional activator of the sulfur pathway. Finally, we found that chromate enters the cells mainly through sulfate transporters and competitively inhibits sulfate uptake. Also consistent with a competition between the two substrates, sulfate supplementation relieves chromate toxicity. However, the data suggest that the chromate-mediated sulfur depletion is not simply due to this competitive uptake but would also be the consequence of competitive metabolism between the two compounds presumably at another step of the sulfur assimilation pathway.
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http://dx.doi.org/10.1093/toxsci/kfn193 | DOI Listing |
J Biol Chem
December 2024
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA. Electronic address:
Glutathione (GSH) is an abundant thiol-containing tripeptide that functions in redox homeostasis, protein folding, and iron metabolism. In Saccharomyces cerevisiae, GSH depletion leads to increased sensitivity to oxidants and other toxic compounds, disruption of Fe-S cluster biogenesis, and eventually cell death. GSH pools are supplied by intracellular biosynthesis and GSH import from the extracellular environment.
View Article and Find Full Text PDFmSystems
December 2024
Department of Bioengineering, University of California, San Diego, California, USA.
Unlabelled: The composition of bacterial transcriptomes is determined by the transcriptional regulatory network (TRN). The TRN regulates the transition from one physiological state to another. Here, we use independent component analysis to monitor the composition of the transcriptome during the transition from the exponential growth phase to the stationary phase.
View Article and Find Full Text PDFWater Res
November 2024
Guangdong Provincial Engineering Research Center for Urban Water Recycling and Environmental Safety, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, Guangdong 518055, PR China; Key Laboratory of Microorganism Application and Risk Control, Ministry of Ecology and Environment, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, Guangdong 518055, PR China; Shenzhen Key Laboratory of Ecological Remediation and Carbon Sequestration, Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen, Guangdong 518055, PR China; Tsinghua University-Kunming Joint Research Center for Dianchi Plateau Lake, Tsinghua University, Beijing 100084, PR China. Electronic address:
Proc Natl Acad Sci U S A
November 2024
Department of Chemistry, University of Massachusetts, Boston, MA 02125.
Sulfur is an essential element for life. Bacteria can obtain sulfur from inorganic sulfate; but in the sulfur starvation-induced response, employ two-component flavin-dependent monooxygenases (TC-FMOs) from the and operons to assimilate sulfur from environmental compounds including alkanesulfonates and dialkylsulfones. Here, we report binding studies of oxidized FMN to enzymes involved within the enzymatic pathway responsible for converting dimethylsulfone (DMSO) to sulfite.
View Article and Find Full Text PDFbioRxiv
October 2024
Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, AL, 35487, USA.
Under conditions of oxidative stress or iron starvation, iron-sulfur cluster biogenesis in is initiated by the cysteine desulfurase, SufS, via the SUF pathway. SufS is a type II cysteine desulfurase that catalyzes the PLP-dependent breakage of an L-cysteine C-S bond to generate L-alanine and a covalent active site persulfide as products. The persulfide is transferred from SufS to SufE and then to the SufBCD complex, which utilizes it in iron-sulfur cluster biogenesis.
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