Evidence map›Paper›PMID 22180625›Full record

ArticleThe Plant cell2011

An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts.

Olaf Czarnecki, Boris Hedtke, Michael Melzer, Maxi Rothbart, Andreas Richter, Yvonne Schröter, Thomas Pfannschmidt, Bernhard Grimm

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.9field-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

55 citing papers in PubMed, 114 citations in OpenAlex.

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  13. An alanine to valine mutation of glutamyl-tRNA reductase enhances 5-aminolevulinic acid synthesis in rice.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2022
    Article
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  15. Bilin-dependent regulation of chlorophyll biosynthesis by GUN4.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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 3 institutions in 1 country.

Olaf CzarneckiDepartment of Plant Physiology, Institute of Biology, Humboldt University Berlin, Berlin, Germany.
Boris Hedtke
Michael Melzer
Maxi Rothbart
Andreas Richter
Yvonne Schröter
Thomas Pfannschmidt
Bernhard Grimm
Humboldt-Universität zu Berlin · DEFriedrich Schiller University Jena · DELeibniz Association · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

5-Aminolevulinic acid (ALA) is the universal precursor for tetrapyrrole biosynthesis and is synthesized in plants in three enzymatic steps: ligation of glutamate (Glu) to tRNA(Glu) by glutamyl-tRNA synthetase, reduction of activated Glu to Glu-1-semialdehyde by glutamyl-tRNA reductase (GluTR), and transamination to ALA by Glu 1-semialdehyde aminotransferase. ALA formation controls the metabolic flow into the tetrapyrrole biosynthetic pathway. GluTR is proposed to be the key regulatory enzyme that is tightly controlled at transcriptional and posttranslational levels. We identified a GluTR binding protein (GluTRBP; previously called PROTON GRADIENT REGULATION7) that is localized in chloroplasts and part of a 300-kD protein complex in the thylakoid membrane. Although the protein does not modulate activity of ALA synthesis, the knockout of GluTRBP is lethal in Arabidopsis thaliana, whereas mutants expressing reduced levels of GluTRBP contain less heme. GluTRBP expression correlates with a function in heme biosynthesis. It is postulated that GluTRBP contributes to subcompartmentalized ALA biosynthesis by maintaining a portion of GluTR at the plastid membrane that funnels ALA into the heme biosynthetic pathway. These results regarding GluTRBP support a model of plant ALA synthesis that is organized in two separate ALA pools in the chloroplast to provide appropriate substrate amounts for balanced synthesis of heme and chlorophyll.

Indexed as

Agrobacterium tumefaciensAldehyde OxidoreductasesAmino Acid SequenceAminolevulinic AcidArabidopsisArabidopsis ProteinsCarrier ProteinsChlorophyllChloroplastsEscherichia coliGene Expression Regulation, PlantGenes, PlantHemeMolecular Sequence DataNicotianaPlants, Genetically ModifiedAldehyde OxidoreductasesAminolevulinic AcidArabidopsis ProteinsCarrier ProteinsChlorophyllglutamyl tRNA reductaseHemeRecombinant ProteinsRNA, PlantThylakoid Membrane Proteins

Identifiers

PMID22180625
PMCPMC3269878
OpenAlexW2123819565

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.