Evidence map›Paper›PMID 16950860›Full record

ArticlePlant physiology2006

Molecular identification of an Arabidopsis S-adenosylmethionine transporter. Analysis of organ distribution, bacterial expression, reconstitution into liposomes, and functional characterization.

Luigi Palmieri, Roberto Arrigoni, Emanuela Blanco, Fernando Carrari, Maria Ines Zanor, Claudia Studart-Guimaraes, Alisdair R Fernie, Ferdinando Palmieri

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 99 citations in OpenAlex.

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  14. MitochondrialFrontiers in plant science · 2019
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  16. Uncoupling proteins 1 and 2 (UCP1 and UCP2) fromThe Journal of biological chemistry · 2018
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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

8 authors at 1 institution in 1 country.

Luigi PalmieriDepartment of Pharmaco-Biology, Laboratory of Biochemistry and Molecular Biology, University of Bari, 70125 Bari, Italy.
Roberto Arrigoni
Emanuela Blanco
Fernando Carrari
Maria Ines Zanor
Claudia Studart-Guimaraes
Alisdair R Fernie
Ferdinando Palmieri
Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite much study of the role of S-adenosylmethionine (SAM) in the methylation of DNA, RNA, and proteins, and as a cofactor for a wide range of biosynthetic processes, little is known concerning the intracellular transport of this essential metabolite. Screening of the Arabidopsis (Arabidopsis thaliana) genome yielded two potential homologs of yeast (Saccharomyces cerevisiae) and human SAM transporters, designated as SAMC1 and SAMC2, both of which belong to the mitochondrial carrier protein family. The SAMC1 gene is broadly expressed at the organ level, although only in specialized tissues of roots with high rates of cell division, and appears to be up-regulated in response to wounding stress, whereas the SAMC2 gene is very poorly expressed in all organs/tissues analyzed. Direct transport assays with the recombinant and reconstituted SAMC1 were utilized to demonstrate that this protein displays a very narrow substrate specificity confined to SAM and its closest analogs. Further experiments revealed that SAMC1 was able to function in uniport and exchange reactions and characterized the transporter as highly active, but sensitive to physiologically relevant concentrations of S-adenosylhomocysteine, S-adenosylcysteine, and adenosylornithine. Green fluorescent protein-based cell biological analysis demonstrated targeting of SAMC1 to mitochondria. Previous proteomic analyses identified this protein also in the chloroplast inner envelope. In keeping with these results, bioinformatics predicted dual localization for SAMC1. These findings suggest that the provision of cytosolically synthesized SAM to mitochondria and possibly also to plastids is mediated by SAMC1 according to the relative demands for this metabolite in the organelles.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsEscherichia coliGene ExpressionGene Expression Regulation, PlantLiposomesMembrane Transport ProteinsMolecular Sequence DataProtein TransportS-AdenosylmethionineSubstrate SpecificityArabidopsis ProteinsLiposomesMembrane Transport ProteinsS-AdenosylmethionineSAMC1 protein, ArabidopsisSAMC2 protein, Arabidopsis

Identifiers

PMID16950860
PMCPMC1630753
OpenAlexW1990458917

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.