Evidence map›Paper›PMID 20023146›Full record

ArticlePlant physiology2010

The missing link in plant histidine biosynthesis: Arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase.

Lindsay N Petersen, Sandra Marineo, Salvatore Mandalà, Faezah Davids, Bryan T Sewell, Robert A Ingle

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
0.9field-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

32 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  8. Review
  9. Article
  10. Article
  11. The Function of Inositol Phosphatases in Plant Tolerance to Abiotic Stress.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Genome ofFrontiers in microbiology · 2017
    Article
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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.

Lindsay N PetersenDepartment of Molecular and Cell Biology, University of Cape Town, Rondebosch 7701, South Africa.
Sandra Marineo
Salvatore Mandalà
Faezah Davids
Bryan T Sewell
Robert A Ingle
University of Cape Town · ZAUniversity of Palermo · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histidine (His) plays a critical role in plant growth and development, both as one of the standard amino acids in proteins, and as a metal-binding ligand. While genes encoding seven of the eight enzymes in the pathway of His biosynthesis have been characterized from a number of plant species, the identity of the enzyme catalyzing the dephosphorylation of histidinol-phosphate to histidinol has remained elusive. Recently, members of a novel family of histidinol-phosphate phosphatase proteins, displaying significant sequence similarity to known myoinositol monophosphatases (IMPs) have been identified from several Actinobacteria. Here we demonstrate that a member of the IMP family from Arabidopsis (Arabidopsis thaliana), myoinositol monophosphatase-like2 (IMPL2; encoded by At4g39120), has histidinol-phosphate phosphatase activity. Heterologous expression of IMPL2, but not the related IMPL1 protein, was sufficient to rescue the His auxotrophy of a Streptomyces coelicolor hisN mutant. Homozygous null impl2 Arabidopsis mutants displayed embryonic lethality, which could be rescued by supplying plants heterozygous for null impl2 alleles with His. In common with the previously characterized HISN genes from Arabidopsis, IMPL2 was expressed in all plant tissues and throughout development, and an IMPL2:green fluorescent protein fusion protein was targeted to the plastid, where His biosynthesis occurs in plants. Our data demonstrate that IMPL2 is the HISN7 gene product, and suggest a lack of genetic redundancy at this metabolic step in Arabidopsis, which is characteristic of the His biosynthetic pathway.

Indexed as

ArabidopsisArabidopsis ProteinsDNA, BacterialDNA, PlantGene Expression Regulation, PlantGenetic Complementation TestHistidineHistidinolHistidinol-PhosphataseModels, MolecularMutagenesis, InsertionalMutationPhosphorylationPhylogenyProtein Structure, TertiaryRecombinant Fusion ProteinsArabidopsis ProteinsDNA, BacterialDNA, PlantHistidineHistidinolHistidinol-PhosphataseRecombinant Fusion ProteinsT-DNA

Identifiers

PMID20023146
PMCPMC2832243
OpenAlexW2098338375

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.