Evidence map›Paper›PMID 15923321›Full record

ArticlePlant physiology2005

The Arabidopsis plastidic methionine sulfoxide reductase B proteins. Sequence and activity characteristics, comparison of the expression with plastidic methionine sulfoxide reductase A, and induction by photooxidative stress.

Christina Vieira Dos Santos, Stéphan Cuiné, Nicolas Rouhier, Pascal Rey

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 158 citations in OpenAlex.

  1. Review
  2. Article
  3. Peptides and Reactive Oxygen Species Regulate Root Development.International journal of molecular sciences · 2025
    Review
  4. Article
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  13. Involvement of the MetO/Msr System in TwoInternational journal of molecular sciences · 2020
    Article
  14. Article
  15. Methionine sulfoxide reductase B fromThe Journal of biological chemistry · 2020
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

2 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

4 authors at 1 institution in 1 country.

Christina Vieira Dos SantosCommissariat à l'Energie Atomique/Cadarache, Direction des Sciences du Vivant, Département d'Ecophysiologie Végétale et de Microbiologie, Laboratoire d'Ecophysiologie de la Photosynthèse, 13108 Saint-Paul-lez-Durance cedex, France.
Stéphan Cuiné
Nicolas Rouhier
Pascal Rey
Institut de Recherches en Technologies et Sciences pour le Vivant · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two types of methionine (Met) sulfoxide reductases (Msr) catalyze the reduction of Met sulfoxide (MetSO) back to Met. MsrA, well characterized in plants, exhibits an activity restricted to the Met-S-SO-enantiomer. Recently, a new type of Msr enzyme, called MsrB, has been identified in various organisms and shown to catalytically reduce the R-enantiomer of MetSO. In plants, very little information is available about MsrB and we focused our attention on Arabidopsis (Arabidopsis thaliana) MsrB proteins. Searching Arabidopsis genome databases, we have identified nine open reading frames encoding proteins closely related to MsrB proteins from bacteria and animal cells. We then analyzed the activity and abundance of the two chloroplastic MsrB proteins, MsrB1 and MsrB2. Both enzymes exhibit an absolute R-stereospecificity for MetSO and a higher catalytic efficiency when using protein-bound MetSO as a substrate than when using free MetSO. Interestingly, we observed that MsrB2 is reduced by thioredoxin, whereas MsrB1 is not. This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction. We investigated the abundance of plastidial MsrA and B in response to abiotic (water stress, photooxidative treatment) and biotic (rust fungus) stresses and we observed that MsrA and B protein levels increase in response to the photooxidative treatment. The possible role of plastidic MsrB in the tolerance to oxidative damage is discussed.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsEnzyme InductionGene Expression Regulation, PlantMethionine Sulfoxide ReductasesMolecular Sequence DataMultigene FamilyMutationOxidative StressOxidoreductasesPlant LeavesPlastidsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidArabidopsis Proteinsmethionine sulfoxide reductaseMethionine Sulfoxide ReductasesOxidoreductasesRecombinant Proteins

Identifiers

PMID15923321
PMCPMC1150407
OpenAlexW2126587228

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.