Dataset Information

Adaptive epigenetic changes in histone variants and modifications rescue the fitness of Arabidopsis plants with dysfunctional histone chaperones

ABSTRACT: The aim was to characterize histone variants and PTMs in mutant plants with histone chaperone dysfunction using mass spectrometry-based approach. We found that the maintenance of genome stability via chromatin remodelling depends on a two-tiered process. The first level relies on a highly flexible mechanism that involves alterations in histone marks while the second adaptive level requires assistance of histone chaperones for the replacement of specific histone variants which is a more time-consuming process.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Gabriela Lochmanova

LAB HEAD: Zbynek Zdrahal

PROVIDER: PXD046034 | Pride | 2024-08-10

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	3905_Lumos4_prop_multiconsensus.pdResult	Other
	3905_Lumos4_prop_multiconsensus.pdResultView	Other
	3905_fas1.msf	Msf
	3905_fas1.raw	Raw
	3905_fas2.msf	Msf

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Publications

Histone Chaperone Deficiency in Arabidopsis Plants Triggers Adaptive Epigenetic Changes in Histone Variants and Modifications.

Franek Michal M Nešpor Dadejová Martina M Pírek Pavlína P Kryštofová Karolína K Dobisová Tereza T Zdráhal Zbyněk Z Dvořáčková Martina M Lochmanová Gabriela G

Molecular & cellular proteomics : MCP 20240605 7

At the molecular scale, adaptive advantages during plant growth and development rely on modulation of gene expression, primarily provided by epigenetic machinery. One crucial part of this machinery is histone posttranslational modifications, which form a flexible system, driving transient changes in chromatin, and defining particular epigenetic states. Posttranslational modifications work in concert with replication-independent histone variants further adapted for transcriptional regulation and ...[more]

PMID: 38848995

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Project description:Propionate is a common three-carbon intermediate produced from the breakdown of propiogenic substrates, such as branched-chain amino acids and odd-numbered fatty acids, and by gut bacteria. Propionate can chemically modify proteins, and if this involves histones, it may underpin a disease-relevant link between short-chain acyls and gene expression in the heart. Here, we sought to characterize how propionate-dependent modifications to histones affect cardiac gene expression and contractile function in a mouse model producing elevated levels of propionate/propionyl-CoA. An adult mouse model of propionic acidaemia (PA) was used to investigate how propionate affects histones and gene expression in the heart, an organ strongly affected in PA patients. Mass spectrometry confirmed elevated plasma propionate in 8-week PA mice, reaching levels detected in PA patient serum. Metabolomic analyses confirmed a metabolic signature of PA, but male mice had enhanced propionate processing towards -alanine. Female PA hearts had expanded end-diastolic and end-systolic volumes, and weaker systolic contractions, without major electrocardiographic changes. Ca2+ signals were deranged in female PA mice (raised diastolic Ca2+), consistent with contractile dysfunction. Differentially-expressed genes (DEGs) included Pde9a and Mme, previously linked to cardiac dysfunction. These DEGs also responded to 48-h culture of wild-type myocytes with propionate as well as butyrate, an HDAC inhibitor, suggesting a role for increased histone acetylation alongside propionylation in inducing these genes. Indeed, histone acetylation (H3K27ac) and propionylation were elevated genome-wide in the PA heart and at the promoters of Pde9a and Mme. These propionate-associated epigenetic responses were more pronounced in female PA mice. The greater prominence of epigenetic, transcriptional, and functional responses in female PA mice, despite a mostly sex-indiscriminate overall metabolic milieu, argues that histone acylation plays a defining role in the cardiac phenotype. We conclude that perturbed propionate metabolism in vivo alters histone acylation and gene expression, which impacts cardiac contractile function.