Evidence map›Paper›PMID 12368503›Full record

ArticleThe Plant cell2002

A polyamine metabolon involving aminopropyl transferase complexes in Arabidopsis.

Mireia Panicot, Eugenio G Minguet, Alejandro Ferrando, Rubén Alcázar, Miguel A Blázquez, Juan Carbonell, Teresa Altabella, Csaba Koncz, Antonio F Tiburcio

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

56 citing papers in PubMed, 180 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

9 authors at 5 institutions in 2 countries.

Mireia PanicotUnitat de Fisiologia Vegetal, Facultat de Farmàcia, Universitat de Barcelona, Diagonal 643, 08028-Barcelona, Spain.
Eugenio G Minguet
Alejandro Ferrando
Rubén Alcázar
Miguel A Blázquez
Juan Carbonell
Teresa Altabella
Csaba Koncz
Antonio F Tiburcio
Universitat de Barcelona · ESInstituto de Biología Molecular y Celular de Plantas · ESMax Planck Institute for Plant Breeding Research · DEConsejo Superior de Investigaciones Científicas · ESMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conversion of putrescine to spermidine in the biosynthetic pathway of plant polyamines is catalyzed by two closely related spermidine synthases, SPDS1 and SPDS2, in Arabidopsis. In the yeast two-hybrid system, SPDS2 was found to interact with SPDS1 and a novel protein, SPMS (spermine synthase), which is homologous with SPDS2 and SPDS1. SPMS interacts with both SPDS1 and SPDS2 in yeast and in vitro. Unlike SPDS1 and SPDS2, SPMS failed to suppress the speDelta3 deficiency of spermidine synthase in yeast. However, SPMS was able to complement the speDelta4 spermine deficiency in yeast, indicating that SPMS is a novel spermine synthase. The SPDS and SPMS proteins showed no homodimerization but formed heterodimers in vitro. Pairwise coexpression of hemagglutinin- and c-Myc epitope-labeled proteins in Arabidopsis cells confirmed the existence of coimmunoprecipitating SPDS1-SPDS2 and SDPS2-SPMS heterodimers in vivo. The epitope-labeled SPDS and SPMS proteins copurified with protein complexes ranging in size from 650 to 750 kD. Our data demonstrate the existence of a metabolon involving at least the last two steps of polyamine biosynthesis in Arabidopsis.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCells, CulturedEpitopesGene Expression Regulation, EnzymologicGenetic Complementation TestMolecular Sequence DataMutationPhylogenyPlant LectinsPolyaminesPrecipitin TestsProtein BindingProtein Interaction MappingArabidopsis ProteinsEpitopesPlant LectinsPolyaminesProto-Oncogene Proteins c-mycPutrescineSPDS1 protein, ArabidopsisSPDS2 protein, ArabidopsisSpermidineSpermidine Synthase

Identifiers

PMID12368503
PMCPMC151234
OpenAlexW2122445449

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.