ArticleThe Biochemical journal2016
CydDC-mediated reductant export in Escherichia coli controls the transcriptional wiring of energy metabolism and combats nitrosative stress.
Article in The Biochemical journal, 2016. 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, 40 citations in OpenAlex.
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- The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli.Redox biology · 2023Article
- Dissecting the conformational complexity and mechanism of a bacterial heme transporter.Nature chemical biology · 2023Article
- Oxidative Reactions Catalyzed by Hydrogen Peroxide Produced by Streptococcus pneumoniae and Other Streptococci Cause the Release and Degradation of Heme from Hemoglobin.Infection and immunity · 2022Article
- Gene essentiality profiling reveals a novel determinant of stresses preventing protein aggregation inEmerging microbes & infections · 2022Article
- Tellurite and Selenite: how can these two oxyanions be chemically different yet so similar in the way they are transformed to their metal forms by bacteria?Biological research · 2022Review
- Recent Advances in Structural Studies of CytochromeInternational journal of molecular sciences · 2022Review
- NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants.Communications biology · 2022Article
- Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics.International journal of molecular sciences · 2021Review
- Proton Pumping and Non-Pumping Terminal Respiratory Oxidases: Active Sites Intermediates of These Molecular Machines and Their Derivatives.International journal of molecular sciences · 2021Review
- Revisiting long-chain fatty acid metabolism in Escherichia coli: integration with stress responses.Current genetics · 2021Review
- Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021Review
- ROS Defense Systems and Terminal Oxidases in Bacteria.Antioxidants (Basel, Switzerland) · 2021Review
- Metabolism of long-chain fatty acids affects disulfide bond formation in Escherichia coli and activates envelope stress response pathways as a combat strategy.PLoS genetics · 2020Article
- CydDC functions as a cytoplasmic cystine reductase to sensitizeProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Bioenergetic Inhibitors: Antibiotic Efficacy and Mechanisms of Action inFrontiers in cellular and infection microbiology · 2020Review
- Sulfur Assimilation Alters Flagellar Function and Modulates the Gene Expression Landscape of Serratia marcescens.mSystems · 2019Article
- NMR metabolomics reveals effects ofGut pathogens · 2019Article
- Restoration of biofuel production levels and increased tolerance under ionic liquid stress is enabled by a mutation in the essential Escherichia coli gene cydC.Microbial cell factories · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The glutathione/cysteine exporter CydDC maintains redox balance in Escherichia coli. A cydD mutant strain was used to probe the influence of CydDC upon reduced thiol export, gene expression, metabolic perturbations, intracellular pH homoeostasis and tolerance to nitric oxide (NO). Loss of CydDC was found to decrease extracytoplasmic thiol levels, whereas overexpression diminished the cytoplasmic thiol content. Transcriptomic analysis revealed a dramatic up-regulation of protein chaperones, protein degradation (via phenylpropionate/phenylacetate catabolism), β-oxidation of fatty acids and genes involved in nitrate/nitrite reduction. (1)H NMR metabolomics revealed elevated methionine and betaine and diminished acetate and NAD(+) in cydD cells, which was consistent with the transcriptomics-based metabolic model. The growth rate and ΔpH, however, were unaffected, although the cydD strain did exhibit sensitivity to the NO-releasing compound NOC-12. These observations are consistent with the hypothesis that the loss of CydDC-mediated reductant export promotes protein misfolding, adaptations to energy metabolism and sensitivity to NO. The addition of both glutathione and cysteine to the medium was found to complement the loss of bd-type cytochrome synthesis in a cydD strain (a key component of the pleiotropic cydDC phenotype), providing the first direct evidence that CydDC substrates are able to restore the correct assembly of this respiratory oxidase. These data provide an insight into the metabolic flexibility of E. coli, highlight the importance of bacterial redox homoeostasis during nitrosative stress, and report for the first time the ability of periplasmic low molecular weight thiols to restore haem incorporation into a cytochrome complex.
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