Evidence map›Paper›PMID 15057280›Full record

ArticleThe EMBO journal2004

Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli.

Benjamin Ezraty, Régis Grimaud, Mohammed El Hassouni, Daniéle Moinier, Frédéric Barras

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

34 citing papers in PubMed, 67 citations in OpenAlex.

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  6. Methionine Redox Homeostasis in Protein Quality Control.Frontiers in molecular biosciences · 2021
    Review
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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

5 authors at 2 institutions in 1 country.

Benjamin EzratyLaboratoire de Chimie Bactérienne, Institut Fédératif de Recherche Biologie Structurale et Microbiologie, Centre National de la Recherche Scientifique, Marseille Cedex, France.
Régis Grimaud
Mohammed El Hassouni
Daniéle Moinier
Frédéric Barras
Centre National de la Recherche Scientifique · FRLaboratoire de Chimie Bactérienne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In proteins, methionine residues are primary targets for oxidation. Methionine oxidation is reversed by methionine sulfoxide reductases A and B, a class of highly conserved enzymes. Ffh protein, a component of the ubiquitous signal recognition particle, contains a methionine-rich domain, interacting with a small 4.5S RNA. In vitro analyses reported here show that: (i) oxidized Ffh is unable to bind 4.5S RNA, (ii) oxidized Ffh contains methionine sulfoxide residues, (iii) oxidized Ffh is a substrate for MsrA and MsrB enzymes; and (iv) MsrA/B repairing activities allow oxidized Ffh to recover 4.5S RNA-binding abilities. In vivo analyses reveal that: (i) Ffh synthesized in the msrA msrB mutant contains methionine sulfoxide residues and is unstable, (ii) msrA msrB mutant requires high levels of Ffh synthesis for growth and (iii) msrA msrB mutation leads to defects in Ffh-dependent targeting of MalF. We conclude that MsrA and MsrB are required to repair Ffh oxidized by reactive oxygen species produced by aerobic metabolism, establishing an as-yet undescribed link between protein targeting and oxidation.

Indexed as

Oxidative StressAmino Acid SequenceEscherichia coliEscherichia coli ProteinsMass SpectrometryMembrane ProteinsMethionine Sulfoxide ReductasesMolecular Sequence DataMutationOxidation-ReductionOxidoreductasesProtein BindingProtein TransportSignal Recognition ParticleSubstrate SpecificityEscherichia coli ProteinsFfh protein, E coliMembrane Proteinsmethionine sulfoxide reductaseMethionine Sulfoxide ReductasesOxidoreductasesSignal Recognition Particle

Identifiers

PMID15057280
PMCPMC394232
OpenAlexW1985700743

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.