Evidence map›Paper›PMID 21599668›Full record

ArticleThe New phytologist2011

Arabidopsis thaliana nucleosidase mutants provide new insights into nucleoside degradation.

Heike Riegler, Claudia Geserick, Rita Zrenner

Open access · bronzeAbstract read
In one paragraph

Article in The New phytologist, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-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

26 citing papers in PubMed, 39 citations in OpenAlex.

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  15. Nucleotide Metabolism in Plants.Plant physiology · 2020
    Article
  16. UMP Kinase Regulates Chloroplast Development and Cold Response in Rice.International journal of molecular sciences · 2019
    Article
  17. Article
  18. Article
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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

3 authors at 1 institution in 1 country.

Heike RieglerMax-Planck-Institute of Molecular Plant Physiology, 14467 Potsdam, Germany.
Claudia GeserickMax-Planck-Institute of Molecular Plant Physiology, 14467 Potsdam, Germany.
Rita ZrennerMax-Planck-Institute of Molecular Plant Physiology, 14467 Potsdam, Germany.
Max Planck Institute of Molecular Plant Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A central step in nucleoside and nucleobase salvage pathways is the hydrolysis of nucleosides to their respective nucleobases. In plants this is solely accomplished by nucleosidases (EC 3.2.2.x). To elucidate the importance of nucleosidases for nucleoside degradation, general metabolism, and plant growth, thorough phenotypic and biochemical analyses were performed using Arabidopsis thaliana T-DNA insertion mutants lacking expression of the previously identified genes annotated as uridine ribohydrolases (URH1 and URH2). Comprehensive functional analyses of single and double mutants demonstrated that both isoforms are unimportant for seedling establishment and plant growth, while one participates in uridine degradation. Rather unexpectedly, nucleoside and nucleotide profiling and nucleosidase activity screening of soluble crude extracts revealed a deficiency of xanthosine and inosine hydrolysis in the single mutants, with substantial accumulation of xanthosine in one of them. Mixing of the two mutant extracts, and by in vitro activity reconstitution using a mixture of recombinant URH1 and URH2 proteins, both restored activity, thus providing biochemical evidence that at least these two isoforms are needed for inosine and xanthosine hydrolysis. This mutant study demonstrates the utility of in vivo systems for the examination of metabolic activities, with the discovery of the new substrate xanthosine and elucidation of a mechanism for expanding the nucleosidase substrate spectrum.

Indexed as

ArabidopsisArabidopsis ProteinsDNA, ComplementaryGene Knockout TechniquesGreen Fluorescent ProteinsHydrolysisInosineMutagenesis, InsertionalN-Glycosyl HydrolasesNucleosidesPhenotypeProtein IsoformsRecombinant Fusion ProteinsRibonucleosidesRNA, PlantSeedlingsArabidopsis ProteinsDNA, ComplementaryGreen Fluorescent ProteinsInosineN-Glycosyl HydrolasesNucleosidesProtein IsoformsRecombinant Fusion ProteinsRibonucleosidesRNA, PlantURH1 protein, ArabidopsisURH2 protein, Arabidopsisuridine nucleosidaseXanthinesxanthosine

Identifiers

PMID21599668
PMCPMC3147060
OpenAlexW2103924847

What OpenQuestion holds

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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.