Evidence map›Paper›PMID 11289508›Full record

ArticlePlant molecular biology2001

Functional characterisation of urease accessory protein G (ureG) from potato.

C P Witte, E Isidore, S A Tiller, H V Davies, M A Taylor

Abstract read
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In one paragraph

Article in Plant molecular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.1field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Interplay of metal ions and urease.Metallomics : integrated biometal science · 2009
    Review
  9. Article
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

C P WitteUnit of Plant Biochemistry, Scottish Crop Research Institute, Invergowrie, Dundee , UK. cwitte@scri.sari.ac.uk
E Isidore
S A Tiller
H V Davies
M A Taylor
James Hutton Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activation of the nickel metalloenzyme urease is a complex process. In bacteria, several urease accessory proteins are essential for incorporation of nickel into the active centre of urease. Comparatively little is known about the activation process and the proteins involved in plants. We cloned five different cDNAs encoding isoforms of urease accessory protein G (ureG) in potato. The 5'-coding region of these cDNAs is highly polymorphic within Solanum tuberosum ssp. tuberosum, containing mainly a simple sequence repeat encoding histidine and aspartate. Mapping on an ultrahigh-density map of the potato genome and Southern blot analysis showed that the isoforms arise from allelic differences of a single-copy gene which was located on chromosome 2. Expression analysis at the mRNA and protein levels indicated the presence of ureG in almost all tissues examined, consistent with the ubiquitous expression of urease. An attempt to correlate urease activity with ureG expression levels in different tissues was made. Allelic copies of ureG were expressed in a tissue-specific manner. UreG from potato and the Klebsiella aerogenes urease operon defective in bacterial ureG were co-expressed in Escherichia coli. The plant gene complements the K. aerogenes ureG mutation, demonstrating that it encodes a urease accessory protein and indicating a structural conservation between the plant and the bacterial urease activation complexes.

Indexed as

Soybean ProteinsAllelesAmino Acid SequenceBase SequenceBlotting, SouthernCarrier ProteinsDNA, ComplementaryDNA, PlantEnterobacter aerogenesGene Expression Regulation, PlantGenetic Complementation TestGTP PhosphohydrolasesMolecular Sequence DataMutationOperonProtein IsoformsCarrier ProteinsDNA, ComplementaryDNA, PlantGTP PhosphohydrolasesProtein IsoformsRNA, MessengerSoybean ProteinsUreaseureG protein, Glycine max

Identifiers

PMID11289508
OpenAlexW146850806

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.