Evidence map›Paper›PMID 35972388›Full record

ArticleThe Plant cell2022

Glutamate 1-semialdehyde aminotransferase is connected to GluTR by GluTR-binding protein and contributes to the rate-limiting step of 5-aminolevulinic acid synthesis.

Neha Sinha, Jürgen Eirich, Iris Finkemeier, Bernhard Grimm

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Ectopic Over-Expression ofPlants (Basel, Switzerland) · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. International journal of molecular sciences · 2023
    Article
  17. Article
  18. 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

4 authors at 1 institution in 1 country.

Neha SinhaInstitute of Biology/Plant Physiology, Humboldt-University Berlin, 10115 Berlin, Germany.ORCID 0000-0002-5589-0309
Jürgen EirichInstitute for Plant Biology and Biotechnology, Plant Physiology, Westfälische Wilhelms-Universität, 48149 Muenster, Germany.ORCID 0000-0003-0963-1872
Iris FinkemeierInstitute for Plant Biology and Biotechnology, Plant Physiology, Westfälische Wilhelms-Universität, 48149 Muenster, Germany.ORCID 0000-0002-8972-4026
Bernhard GrimmInstitute of Biology/Plant Physiology, Humboldt-University Berlin, 10115 Berlin, Germany.ORCID 0000-0002-9730-1074
Humboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetrapyrroles play fundamental roles in crucial processes including photosynthesis, respiration, and catalysis. In plants, 5-aminolevulinic acid (ALA) is the common precursor of tetrapyrroles. ALA is synthesized from activated glutamate by the enzymes glutamyl-tRNA reductase (GluTR) and glutamate-1-semialdehyde aminotransferase (GSAAT). ALA synthesis is recognized as the rate-limiting step in this pathway. We aimed to explore the contribution of GSAAT to the control of ALA synthesis and the formation of a protein complex with GluTR. In Arabidopsis thaliana, two genes encode GSAAT isoforms: GSA1 and GSA2. A comparison of two GSA knockout mutants with the wild-type revealed the correlation of reduced GSAAT activity and ALA-synthesizing capacity in leaves with lower chlorophyll content. Growth and green pigmentation were more severely impaired in gsa2 than in gsa1, indicating the predominant role of GSAAT2 in ALA synthesis. Interestingly, GluTR accumulated to higher levels in gsa2 than in the wild-type and was mainly associated with the plastid membrane. We propose that the GSAAT content modulates the amount of soluble GluTR available for ALA synthesis. Several different biochemical approaches revealed the GSAAT-GluTR interaction through the assistance of GluTR-binding protein (GBP). A modeled structure of the tripartite protein complex indicated that GBP mediates the stable association of GluTR and GSAAT for adequate ALA synthesis.

Indexed as

Aldehyde OxidoreductasesAminolevulinic AcidArabidopsisArabidopsis ProteinsIntramolecular TransferasesTransaminasesCarrier ProteinsGlutamatesTetrapyrrolesAldehyde OxidoreductasesAminolevulinic AcidArabidopsis ProteinsCarrier Proteinsglutamate-1-semialdehyde 2,1-aminomutaseGlutamatesglutamyl tRNA reductaseglutamyl-tRNA reductase, Arabidopsisglutamyl-tRNA reductase-binding protein, ArabidopsisIntramolecular TransferasesTetrapyrrolesTransaminases

Identifiers

PMID35972388
PMCPMC9614494
OpenAlexW4292064616

What OpenQuestion holds

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LicenceCC BY
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.