ArticleThe Journal of biological chemistry2013
Redox proteomics uncovers peroxynitrite-sensitive proteins that help Escherichia coli to overcome nitrosative stress.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Strategies to Enhance the Efficacy and Clinical Translation of Antimicrobial Photodynamic Therapy.Antibiotics (Basel, Switzerland) · 2026Review
- Regulation of titin-based cardiac stiffness by unfolded domain oxidation (UnDOx).Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.Microbiology and molecular biology reviews : MMBR · 2020Review
- Bacterial Defense Systems against the Neutrophilic Oxidant Hypochlorous Acid.Infection and immunity · 2020Review
- Quantifying changes in the bacterial thiol redox proteome during host-pathogen interaction.Redox biology · 2019Article
- Antimicrobial Efficacy and Safety of a Novel Gas Plasma-Activated Catheter Lock Solution.Antimicrobial agents and chemotherapy · 2018Article
- Maintaining a Healthy Proteome during Oxidative Stress.Molecular cell · 2018Review
- Stress-Activated Chaperones: A First Line of Defense.Trends in biochemical sciences · 2017Review
- Protein quality control under oxidative stress conditions.Journal of molecular biology · 2015Review
- Activation of RidA chaperone function by N-chlorination.Nature communications · 2014Article
- Functional metagenomics of the thioredoxin superfamily.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxynitrite is a highly reactive chemical species with antibacterial properties that are synthesized in immune cells. In a proteomic approach, we identified specific target proteins of peroxynitrite-induced modifications in Escherichia coli. Although peroxynitrite caused a fairly indiscriminate nitration of tyrosine residues, reversible modifications of protein thiols were highly specific. We used a quantitative redox proteomic method based on isotope-coded affinity tag chemistry and identified four proteins consistently thiol-modified in cells treated with peroxynitrite as follows: AsnB, FrmA, MaeB, and RidA. All four were required for peroxynitrite stress tolerance in vivo. Three of the identified proteins were modified at highly conserved cysteines, and MaeB and FrmA are known to be directly involved in the oxidative and nitrosative stress response in E. coli. In in vitro studies, we could show that the activity of RidA, a recently discovered enamine/imine deaminase, is regulated in a specific manner by the modification of its single conserved cysteine. Mutation of this cysteine 107 to serine generated a constitutively active protein that was not susceptible to peroxynitrite.
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