Evidence map›Paper›PMID 23690622›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Methionine oxidation activates a transcription factor in response to oxidative stress.

Adrian Drazic, Haruko Miura, Jirka Peschek, Yan Le, Nina C Bach, Thomas Kriehuber, Jeannette Winter

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
6.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

90 citing papers in PubMed, 157 citations in OpenAlex.

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  20. Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022
    Review

30 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Adrian DrazicCenter for Integrated Protein Science Munich, Department Chemie, Technische Universität München, 85747 Garching, Germany.
Haruko Miura
Jirka Peschek
Yan Le
Nina C Bach
Thomas Kriehuber
Jeannette Winter
Technical University of Munich · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidant-mediated antibacterial response systems are broadly used to control bacterial proliferation. Hypochlorite (HOCl) is an important component of the innate immune system produced in neutrophils and specific epithelia. Its antimicrobial activity is due to damaging cellular macromolecules. Little is known about how bacteria escape HOCl-inflicted damage. Recently, the transcription factor YjiE was identified that specifically protects Escherichia coli from HOCl killing. According to its function, YjiE is now renamed HypT (hypochlorite-responsive transcription factor). Here we unravel that HypT is activated by methionine oxidation to methionine sulfoxide. Interestingly, so far only inactivation of cellular proteins by methionine oxidation has been reported. Mutational analysis revealed three methionines that are essential to confer HOCl resistance. Their simultaneous substitution by glutamine, mimicking the methionine sulfoxide state, increased the viability of E. coli cells upon HOCl stress. Triple glutamine substitution generates a constitutively active HypT that regulates target genes independently of HOCl stress and permanently down-regulates intracellular iron levels. Inactivation of HypT depends on the methionine sulfoxide reductases A/B. Thus, microbial protection mechanisms have evolved along the evolution of antimicrobial control systems, allowing bacteria to survive within the host environment.

Indexed as

Models, MolecularAmino Acid SequenceBase SequenceBlotting, WesternChromatography, GelDNA Mutational AnalysisEscherichia coliEscherichia coli ProteinsEvolution, MolecularHypochlorous AcidImmunity, InnateIronMass SpectrometryMethionineMolecular Sequence DataMutagenesisEscherichia coli ProteinsHypochlorous AcidHypT protein, E coliIronMethionineRepressor ProteinsLysR-type transcription factorMsrAMsrBposttranslational modification

Identifiers

PMID23690622
PMCPMC3677443
OpenAlexW2117141398

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.