ArticleMolecular microbiology2020
Cystine import is a valuable but risky process whose hazards Escherichia coli minimizes by inducing a cysteine exporter.
Article in Molecular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 58 citations in OpenAlex.
- The Effect of Hydrogen Sulfide and Reactive Sulfur Species on Bacterial Virulence and Antibiotic Sensitivity.International journal of molecular sciences · 2026Review
- Anaerobic sulfide removal involves an intricate interplay between biomass, biosulfur, and solutes.Environmental science : water research & technology · 2026Article
- Activation of the Spx redox sensor counters cysteine-driven Fe(II) depletion under disulfide stress.bioRxiv : the preprint server for biology · 2025Article
- Ammonium depletion induces changes in low molecular weight thiol levels in Escherichia coli and Bacillus subtilis.Archives of microbiology · 2025Article
- Discovery of a Widespread Polyamine-Low-Molecular-Weight Thiol Hybrid Pathway inACS infectious diseases · 2025Article
- Article
- Sulphur-Acquisition Pathways for Cysteine Synthesis Confer a Fitness Advantage to Bacteria in Plant Extracts.Environmental microbiology · 2025Article
- Experimental evolution ofMicrobiology spectrum · 2025Article
- Coenzyme A metabolism: a key driver of gut microbiota dynamics and metabolic profiles.FEMS microbiology reviews · 2025Review
- Synergistic action between peptide-neomycin conjugates and polymyxin B against multidrug-resistant gram-negative pathogens.Frontiers in microbiology · 2025Article
- Exogenous cystine increases susceptibility of drug-resistantFrontiers in microbiology · 2025Article
- Effect of HArchives of microbiology · 2024Article
- Bioluminescence-Based Determination of Cytosolic Accumulation of Antibiotics inACS infectious diseases · 2024Article
- Regulation of Cysteine Homeostasis and Its Effect onInternational journal of molecular sciences · 2024Article
- Article
- Physiological and genomic evidence of cysteine degradation and aerobic hydrogen sulfide production in freshwater bacteria.mSystems · 2023Article
- Influence of Growth Medium Composition on Physiological Responses ofBiotech (Basel (Switzerland)) · 2023Article
- Excess copper catalyzes protein disulfide bond formation in the bacterial periplasm but not in the cytoplasm.Molecular microbiology · 2023Article
- Identifying the mediators of intracellular E. coli inactivation under UVA light: The (photo) Fenton process and singlet oxygen.Water research · 2022Article
- Rhodaneses minimize the accumulation of cellular sulfane sulfur to avoid disulfide stress during sulfide oxidation in bacteria.Redox biology · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The structure of free cysteine makes it vulnerable to oxidation by molecular oxygen; consequently, organisms that live in oxic habitats have acquired the ability to import cystine as a sulfur source. We show that cystine imported into Escherichia coli can transfer disulfide bonds to cytoplasmic proteins. To minimize this problem, the imported cystine is rapidly reduced. However, this conversion of cystine to cysteine precludes product inhibition of the importer, so cystine import continues into cells that are already sated with cysteine. The burgeoning cysteine pool is itself hazardous, as cysteine promotes the formation of reactive oxygen species, triggers sulfide production and competitively inhibits a key enzyme in the isoleucine biosynthetic pathway. The Lrp transcription factor senses the excess cysteine and induces AlaE, an export protein that pumps cysteine back out of the cell until transcriptional controls succeed in lowering the amount of the importer. While it lasts, the overall phenomenon roughly doubles the NADPH demand of the cell. It comprises another example of the incompatibility of the reduced cytoplasms of microbes with the oxic world in which they dwell. It also reveals one natural source of cytoplasmic disulfide stress and sheds light on a role for broad-spectrum amino acid exporters.
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