Evidence map›Paper›PMID 26100864›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Osmotic stress induces phosphorylation of histone H3 at threonine 3 in pericentromeric regions of Arabidopsis thaliana.

Zhen Wang, Juan Armando Casas-Mollano, Jianping Xu, Jean-Jack M Riethoven, Chi Zhang, Heriberto Cerutti

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
18.1field-weighted citation impact, top 1% 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

50 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Mitotic Disruption and Cytoskeletal Alterations Induced byInternational journal of molecular sciences · 2025
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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 1 institution in 1 country.

Zhen WangSchool of Biological Sciences and Center for Plant Science Innovation, University of Nebraska, Lincoln, NE 68588;
Juan Armando Casas-MollanoSchool of Biological Sciences and Center for Plant Science Innovation, University of Nebraska, Lincoln, NE 68588;
Jianping XuSchool of Biological Sciences and Center for Plant Science Innovation, University of Nebraska, Lincoln, NE 68588;
Jean-Jack M RiethovenCenter for Biotechnology, University of Nebraska, Lincoln, NE 68588.ORCID http://orcid.org/0000-0002-2709-7880
Chi ZhangSchool of Biological Sciences and Center for Plant Science Innovation, University of Nebraska, Lincoln, NE 68588;
Heriberto CeruttiSchool of Biological Sciences and Center for Plant Science Innovation, University of Nebraska, Lincoln, NE 68588; hcerutti1@unl.edu.
University of Nebraska–Lincoln · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone phosphorylation plays key roles in stress-induced transcriptional reprogramming in metazoans but its function(s) in land plants has remained relatively unexplored. Here we report that an Arabidopsis mutant defective in At3g03940 and At5g18190, encoding closely related Ser/Thr protein kinases, shows pleiotropic phenotypes including dwarfism and hypersensitivity to osmotic/salt stress. The double mutant has reduced global levels of phosphorylated histone H3 threonine 3 (H3T3ph), which are not enhanced, unlike the response in the wild type, by drought-like treatments. Genome-wide analyses revealed increased H3T3ph, slight enhancement in trimethylated histone H3 lysine 4 (H3K4me3), and a modest decrease in histone H3 occupancy in pericentromeric/knob regions of wild-type plants under osmotic stress. However, despite these changes in heterochromatin, transposons and repeats remained transcriptionally repressed. In contrast, this reorganization of heterochromatin was mostly absent in the double mutant, which exhibited lower H3T3ph levels in pericentromeric regions even under normal environmental conditions. Interestingly, within actively transcribed protein-coding genes, H3T3ph density was minimal in 5' genic regions, coincidental with a peak of H3K4me3 accumulation. This pattern was not affected in the double mutant, implying the existence of additional H3T3 protein kinases in Arabidopsis. Our results suggest that At3g03940 and At5g18190 are involved in the phosphorylation of H3T3 in pericentromeric/knob regions and that this repressive epigenetic mark may be important for maintaining proper heterochromatic organization and, possibly, chromosome function(s).

Indexed as

ArabidopsisArabidopsis ProteinsCentromereChromosomes, PlantGene Expression Regulation, PlantHeterochromatinHistonesImmunoblottingLysineMethylationMutationOsmotic PressurePhosphorylationPlants, Genetically ModifiedProtein Serine-Threonine KinasesReverse Transcriptase Polymerase Chain ReactionArabidopsis ProteinsHeterochromatinHistonesLysineMLK1 protein, ArabidopsisMLK2 protein, ArabidopsisProtein Serine-Threonine KinasesSodium ChlorideThreonineabiotic stressepigeneticsheterochromatinhistone phosphorylationprotein kinase

Identifiers

PMID26100864
PMCPMC4500206
OpenAlexW1525160146

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.