Evidence map›Paper›PMID 14551326›Full record

ArticlePlant physiology2003

PRT1 of Arabidopsis is a ubiquitin protein ligase of the plant N-end rule pathway with specificity for aromatic amino-terminal residues.

Susanne Stary, Xiao-jun Yin, Thomas Potuschak, Peter Schlögelhofer, Victoria Nizhynska, Andreas Bachmair

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

39 citing papers in PubMed, 82 citations in OpenAlex.

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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

6 authors at 2 institutions in 2 countries.

Susanne StaryInstitute of Botany, University of Vienna, Rennweg 14, A-1030 Vienna, Austria.
Xiao-jun Yin
Thomas Potuschak
Peter Schlögelhofer
Victoria Nizhynska
Andreas Bachmair
University of Vienna · ATMax Planck Institute for Plant Breeding Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gene PRT1 of Arabidopsis, encoding a 45-kD protein with two RING finger domains, is essential for the degradation of F-dihydrofolate reductase, a model substrate of the N-end rule pathway of protein degradation. We have determined the function of PRT1 by expression in yeast (Saccharomyces cerevisiae). PRT1 can act as a ubiquitin protein ligase in the heterologous host. The identified substrates of PRT1 have an aromatic residue at their amino-terminus, indicating that PRT1 mediates degradation of N-end rule substrates with aromatic termini but not of those with aliphatic or basic amino-termini. Expression of model substrates in mutant and wild-type plants confirmed this substrate specificity. A ligase activity exclusively devoted to aromatic amino-termini of the N-end rule pathway is apparently unique to plants. The results presented also imply that other known substrates of the plant N-end rule pathway are ubiquitylated by one or more different ubiquitin protein ligases.

Indexed as

Amino Acids, AromaticArabidopsisArabidopsis ProteinsDNA-Binding ProteinsEnzyme InhibitorsGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMutationSaccharomyces cerevisiaeSubstrate SpecificityTetrahydrofolate DehydrogenaseUbiquitin-Protein LigasesAmino Acids, AromaticArabidopsis ProteinsDNA-Binding ProteinsEnzyme InhibitorsPRT1 protein, ArabidopsisTetrahydrofolate DehydrogenaseUbiquitin-Protein Ligases

Identifiers

PMID14551326
PMCPMC281630
OpenAlexW2152145418

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.