Evidence map›Paper›PMID 19293370›Full record

ArticleThe Plant cell2009

Uridine-ribohydrolase is a key regulator in the uridine degradation pathway of Arabidopsis.

Benjamin Jung, Martin Flörchinger, Hans-Henning Kunz, Michaela Traub, Ruth Wartenberg, Wolfgang Jeblick, H Ekkehard Neuhaus, Torsten Möhlmann

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  4. A cell wall-localized cytokinin/purine riboside nucleosidase is involved in apoplastic cytokinin metabolism inProceedings of the National Academy of Sciences of the United States of America · 2023
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  16. Nucleotide Metabolism in Plants.Plant physiology · 2020
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  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Benjamin JungAbteilung Pflanzenphysiologie, Fachbereich Biologie, Technische Universität Kaiserslautern, D-67663 Kaiserslautern, Germany.
Martin Flörchinger
Hans-Henning Kunz
Michaela Traub
Ruth Wartenberg
Wolfgang Jeblick
H Ekkehard Neuhaus
Torsten Möhlmann
University of Kaiserslautern · DEUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleoside degradation and salvage are important metabolic pathways but hardly understood in plants. Recent work on human pathogenic protozoans like Leishmania and Trypanosoma substantiates an essential function of nucleosidase activity. Plant nucleosidases are related to those from protozoans and connect the pathways of nucleoside degradation and salvage. Here, we describe the cloning of such an enzyme from Arabidopsis thaliana, Uridine-Ribohydrolase 1 (URH1) and the characterization by complementation of a yeast mutant. Furthermore, URH1 was synthesized as a recombinant protein in Escherichia coli. The pure recombinant protein exhibited highest hydrolase activity for uridine, followed by inosine and adenosine, the corresponding K(m) values were 0.8, 1.4, and 0.7 mM, respectively. In addition, URH1 was able to cleave the cytokinin derivative isopentenyladenine-riboside. Promoter beta-glucuronidase fusion studies revealed that URH1 is mainly transcribed in the vascular cells of roots and in root tips, guard cells, and pollen. Mutants expressing the Arabidopsis enzyme or the homolog from rice (Oryza sativa) exhibit resistance toward toxic fluorouridine, fluorouracil, and fluoroorotic acid, providing clear evidence for a pivotal function of URH1 as regulative in pyrimidine degradation. Moreover, mutants with increased and decreased nucleosidase activity are delayed in germination, indicating that this enzyme activity must be well balanced in the early phase of plant development.

Indexed as

Amino Acid SequenceAnthocyaninsArabidopsisArabidopsis ProteinsArginineGenetic Complementation TestHumansIsoenzymesMolecular Sequence DataMutationN-Glycosyl HydrolasesNitrogenPlants, Genetically ModifiedRecombinant Fusion ProteinsSequence AlignmentUridineAnthocyaninsArabidopsis ProteinsArginineIsoenzymesN-Glycosyl HydrolasesNitrogenRecombinant Fusion ProteinsURH1 protein, ArabidopsisUridineuridine nucleosidase

Identifiers

PMID19293370
PMCPMC2671717
OpenAlexW2122514636

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.