Evidence map›Paper›PMID 25837721›Full record

ArticlePloS one2015

Uptake of L-cystine via an ABC transporter contributes defense of oxidative stress in the L-cystine export-dependent manner in Escherichia coli.

Iwao Ohtsu, Yusuke Kawano, Marina Suzuki, Susumu Morigasaki, Kyohei Saiki, Shunsuke Yamazaki, Gen Nonaka, Hiroshi Takagi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 70 citations in OpenAlex.

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  20. Optimization ofPathogens (Basel, Switzerland) · 2021
    Article
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

8 authors at 2 institutions in 1 country.

Iwao OhtsuGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Yusuke KawanoGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Marina SuzukiGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Susumu MorigasakiGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Kyohei SaikiGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Shunsuke YamazakiResearch Institute for Bioscience Products and Fine Chemicals, Ajinomoto Company, Kawasaki, Kanagawa, Japan.
Gen NonakaResearch Institute for Bioscience Products and Fine Chemicals, Ajinomoto Company, Kawasaki, Kanagawa, Japan.
Hiroshi TakagiGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.
Nara Institute of Science and Technology · JPAjinomoto (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular thiols like L-cystine and L-cystine play a critical role in the regulation of cellular processes. Here we show that Escherichia coli has two L-cystine transporters, the symporter YdjN and the ATP-binding cassette importer FliY-YecSC. These proteins import L-cystine, an oxidized product of L-cystine from the periplasm to the cytoplasm. The symporter YdjN, which is expected to be a new member of the L-cystine regulon, is a low affinity L-cystine transporter (Km = 1.1 μM) that is mainly involved in L-cystine uptake from outside as a nutrient. E. coli has only two L-cystine importers because ΔydjNΔyecS mutant cells are not capable of growing in the minimal medium containing L-cystine as a sole sulfur source. Another protein YecSC is the FliY-dependent L-cystine transporter that functions cooperatively with the L-cystine transporter YdeD, which exports L-cystine as reducing equivalents from the cytoplasm to the periplasm, to prevent E. coli cells from oxidative stress. The exported L-cystine can reduce the periplasmic hydrogen peroxide to water, and then generated L-cystine is imported back into the cytoplasm via the ATP-binding cassette transporter YecSC with a high affinity to L-cystine (Km = 110 nM) in a manner dependent on FliY, the periplasmic L-cystine-binding protein. The double disruption of ydeD and fliY increased cellular levels of lipid peroxides. From these findings, we propose that the hydrogen peroxide-inducible L-cystine/L-cystine shuttle system plays a role of detoxification of hydrogen peroxide before lipid peroxidation occurs, and then might specific prevent damage to membrane lipids.

Indexed as

Oxidative StressAdaptation, BiologicalATP-Binding Cassette TransportersBiological TransportCystineEscherichia coliGene OrderGenes, BacterialGenetic LociHydrogen PeroxideKineticsLipid PeroxidationMembrane LipidsModels, BiologicalMutationATP-Binding Cassette TransportersCystineHydrogen PeroxideMembrane Lipids

Identifiers

PMID25837721
PMCPMC4383340
OpenAlexW2087312505

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.