Evidence map›Paper›PMID 40200022›Full record

ArticleNature plants2025

An Oryza-specific histone H4 variant predisposes H4 lysine 5 acetylation to modulate salt stress responses.

Vivek Hari-Sundar Gandhivel, Paula Sotelo-Parrilla, Steffi Raju, Shaileshanand Jha, Anjitha Gireesh, Chitthavalli Y Harshith, Fabian Gut, Kutti R Vinothkumar, Frédéric Berger, A Arockia Jeyaprakash and 1 more

Abstract read
In one paragraph

Article in Nature plants, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Review
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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

11 authors.

Vivek Hari-Sundar GandhivelNational Centre for Biological Sciences, TIFR, GKVK Campus, Bangalore, India.ORCID 0000-0002-7919-0550
Paula Sotelo-ParrillaGene Center and Department of Biochemistry, Ludwig-Maximilian-Universität, Munich, Germany.ORCID 0000-0002-6333-1005
Steffi RajuNational Centre for Biological Sciences, TIFR, GKVK Campus, Bangalore, India.
Shaileshanand JhaNational Centre for Biological Sciences, TIFR, GKVK Campus, Bangalore, India.
Anjitha GireeshCentre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, UK.ORCID 0000-0003-1727-1053
Chitthavalli Y HarshithNational Centre for Biological Sciences, TIFR, GKVK Campus, Bangalore, India.
Fabian GutGene Center and Department of Biochemistry, Ludwig-Maximilian-Universität, Munich, Germany.
Kutti R VinothkumarNational Centre for Biological Sciences, TIFR, GKVK Campus, Bangalore, India.ORCID 0000-0002-6746-5684
Frédéric BergerGregor Mendel Institute of Molecular Plant Biology, Austrian Academy of Sciences, Vienna, Austria.ORCID 0000-0002-3609-8260
A Arockia JeyaprakashGene Center and Department of Biochemistry, Ludwig-Maximilian-Universität, Munich, Germany.ORCID 0000-0002-1889-8635
P V ShivaprasadNational Centre for Biological Sciences, TIFR, GKVK Campus, Bangalore, India. shivaprasad@ncbs.res.in.ORCID 0000-0002-9296-4848

Funding

Department of Atomic Energy, Government of India (DAE) RTI 4006 (1303/3/2019/R&D-II/DAE/4749 dated 16.7.2020)Department of Biotechnology, Ministry of Science and Technology (DBT) BT/IN/Swiss/47/JGK/2018-19DST | Science and Engineering Research Board (SERB) CRG/2023/003849European Research Council 101054950Wellcome TrustWellcome Trust 202811
6 · The paper itself

Abstract

Paralogous variants of canonical histones guide accessibility to DNA and function as additional layers of genome regulation. Across eukaryotes, the mechanism of action and functional significance of several variants of core histones are well known except those of histone H4. Here we show that a variant of H4 (H4.V) expressing tissue-specifically among Oryza members mediated specific epigenetic changes contributing to salt tolerance. H4.V was incorporated into specific heterochromatic sites, where it blocked the deposition of active histone marks. Stress-dependent redistribution of H4.V enabled the incorporation of acetylated H4 lysine 5 (H4K5ac) in the gene bodies. The misexpression of H4.V led to defects in reproductive development and in mounting salt stress responses. H4.V formed homotypic nucleosomes and mediated these alterations by conferring distinct molecular properties to the nucleosomes, as seen with cryo electron microscopy structures and biochemical assays. These results reveal not only an H4 variant among plants but also a chromatin regulation that might have contributed to the adaptation of semi-aquatic Oryza members.

Indexed as

HistonesLysineOryzaPlant ProteinsSalt StressAcetylationEpigenesis, GeneticNucleosomesSalt ToleranceHistonesLysineNucleosomesPlant Proteins

Identifiers

PMID40200022
PMCPMC7617672

What Socratic holds

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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 Socratic graph.