Evidence map›Paper›PMID 39576594›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Quantitative Profiling of Histone Variants and Posttranslational Modifications by Tandem Mass Spectrometry in Arabidopsis.

Vangeli Geshkovski, Hassan Hijazi, Julie Manessier, Sabine Brugière, Marie Courçon, Gilles Vachon, Delphine Pflieger, Cristel C Carles

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Enhanced plant bottom-up histone proteomics.Journal of experimental botany · 2026
    Article
  3. 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

8 authors.

Vangeli GeshkovskiGrenoble Alpes University-CNRS-INRAE-CEA, Plant and Cell Physiology Lab (LPCV), IRIG-DBSCI, Grenoble, France.ORCID 0000-0001-9474-4382
Hassan HijaziUniversity Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, FR2048, Grenoble, France.
Julie ManessierUniversity Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, FR2048, Grenoble, France.
Sabine BrugièreUniversity Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, FR2048, Grenoble, France.
Marie CourçonUniversity Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, FR2048, Grenoble, France.ORCID 0000-0001-7152-1768
Gilles VachonGrenoble Alpes University-CNRS-INRAE-CEA, Plant and Cell Physiology Lab (LPCV), IRIG-DBSCI, Grenoble, France.
Delphine PfliegerUniversity Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, FR2048, Grenoble, France. Delphine.pflieger@cea.fr.ORCID 0000-0003-2122-3900
Cristel C CarlesGrenoble Alpes University-CNRS-INRAE-CEA, Plant and Cell Physiology Lab (LPCV), IRIG-DBSCI, Grenoble, France. Christel.carles@univ-grenoble-alpes.fr.ORCID 0000-0002-9416-4860

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone dynamics constitute an important layer of gene regulations associated with development and growth in multicellular eukaryotes. They also stand as key determinants of plant responses to environmental changes. Histone dynamics include the exchange of histone variants as well as post-translational modifications of their amino acid residues (such as acetylation and mono/di/trimethylation), commonly referred to as histone marks. Investigating histone dynamics with a focus on combinatorial changes occurring at their residues will greatly help unravel how plants achieve phenotypic plasticity.Mass spectrometry (MS) analysis offers unequaled resolution of the abundance of histone variants and of their marks. Indeed, relative to other techniques such as western blot or genome-wide profiling, this powerful technique allows quantifying the relative abundances of histone forms, as well as revealing coexisting marks on the same histone molecule. Yet, while MS-based histone analysis has proven efficient in several animals and other model organisms, this method stands out as more challenging in plants. One major challenge is the isolation of sufficient amounts of pure, high-quality histones, likely rendered difficult by the presence of the cell wall, for sufficiently deep and resolutive identification of histone species.In this chapter, we describe a straightforward MS-based proteomic method, implemented to characterize histone marks from Arabidopsis thaliana seedling tissues and cell culture suspensions. After acid extraction of histones, in vitro propionylation of free lysine residues, and digestion with trypsin, a treatment at highly basic pH allows obtaining sharp spectral signals of biologically relevant histone peptide forms.The method workflow described here shall be used to measure changes in histone marks between Arabidopsis thaliana genotypes, along developmental time-courses, or upon various stresses and treatments.

Indexed as

ArabidopsisHistonesProtein Processing, Post-TranslationalTandem Mass SpectrometryArabidopsis ProteinsChromatography, LiquidHistone CodeProteomicsArabidopsis ProteinsHistonesAcid precipitationArabidopsis thalianaChromatin marksEpigeneticsHistone H3Histone variantsLysine modificationsLysine propionylationPlant cell culture suspensionReversing excessive propionylationSeedlingsTandem mass spectrometry

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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.