Evidence map›Paper›PMID 26063505›Full record

ArticlePlant physiology2015

Analysis of Loss-of-Function Mutants in Aspartate Kinase and Homoserine Dehydrogenase Genes Points to Complexity in the Regulation of Aspartate-Derived Amino Acid Contents.

Teresa J Clark, Yan Lu

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
5.2field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Genome-wide identification of theFrontiers in plant science · 2026
    Article
  3. Article
  4. Article
  5. New Insight into Aspartate Metabolic Pathways inInternational journal of molecular sciences · 2022
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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

2 authors at 1 institution in 1 country.

Teresa J ClarkDepartment of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410.ORCID http://orcid.org/0000-0002-8396-8388
Yan LuDepartment of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410 yan.1.lu@wmich.edu.ORCID http://orcid.org/0000-0002-3374-7376
Western Michigan University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biosynthesis of aspartate (Asp)-derived amino acids lysine (Lys), methionine (Met), threonine (Thr), and isoleucine involves monofunctional Asp kinases (AKs) and dual-functional Asp kinase-homoserine dehydrogenases (AK-HSDHs). Four-week-old loss-of-function Arabidopsis (Arabidopsis thaliana) mutants in the AK-HSDH2 gene had increased amounts of Asp and Asp-derived amino acids, especially Thr, in leaves. To explore mechanisms behind this phenotype, we obtained single mutants for other AK and AK-HSDH genes, generated double mutants from ak-hsdh2 and ak mutants, and performed free and protein-bound amino acid profiling, transcript abundance, and activity assays. The increases of Asp, Lys, and Met in ak-hsdh2 were also observed in ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 was observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Activity assays showed that AK2 and AK-HSDH1 are the major contributors to overall AK and HSDH activities, respectively. Pairwise correlation analysis revealed positive correlations between the amount of AK transcripts and Lys-sensitive AK activity and between the amount of AK-HSDH transcripts and both Thr-sensitive AK activity and total HSDH activity. In addition, the ratio of total AK activity to total HSDH activity negatively correlates with the ratio of Lys to the total amount of Met, Thr, and isoleucine. These data led to the hypothesis that the balance between Lys-sensitive AKs and Thr-sensitive AK-HSDHs is important for maintaining the amounts and ratios of Asp-derived amino acids.

Indexed as

MutationAmino AcidsArabidopsisArabidopsis ProteinsAspartate KinaseAspartic AcidAspartokinase Homoserine DehydrogenaseChromatography, High Pressure LiquidGene Expression Regulation, EnzymologicGene Expression Regulation, PlantImmunoblottingIsoenzymesLysineMethioninePlant LeavesReverse Transcriptase Polymerase Chain ReactionAmino AcidsArabidopsis ProteinsAspartate KinaseAspartic AcidAspartokinase Homoserine DehydrogenaseIsoenzymesLysineMethionineThreonine

Identifiers

PMID26063505
PMCPMC4528744
OpenAlexW1946024497

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.