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Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury

ABSTRACT: Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury

PROVIDER: PRJNA1263501 | ENA |

REPOSITORIES: ENA

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Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury [RNA-seq]

Project description:Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury [RNA-seq]

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Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury [ChIP-seq]

Project description:Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury [ChIP-seq]

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Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury [RNA-seq]

Project description:The intestinal epithelium undergoes rapid turnover driven by Lgr5+ intestinal stem cells (ISCs) at the crypt base, and can recover despite ISC loss during damage. However, the role of epigenetic modifications in regulating this regeneration remains unclear. In this study, we report that H3K14 crotonylation (H3K14cr), a vital histone modification mediated by the acyltransferase HBO1, is essential for intestinal regeneration. HBO1 ablation in the intestinal epithelium exacerbates dextran sulfate sodium (DSS)-induced colitis.

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Crotonate-activated histone H3K14 crotonylation enhances intestinal regeneration after injury

Project description:This SuperSeries is composed of the SubSeries listed below.

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Effect of Crotonylation in the development of glioma

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Project description:In this study we report that histone crotonylation promotes human embryonic stem cell differentiation to endoderm cells. Addition of crotonate, a precursor for crotonyl-CoA and therefore histone crotonylation, dramatically enhanced endoderm cell differentiation from human embryonic stem cells, while incubation of acetate, a precursor of acetyl-CoA and therefore histone acetylation, did not change the efficiency of endoderm differentiation.

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Project description:Protein acetylation and crotonylation are important post-translational modifications (PTMs) of lysine. In animal cells, histone lysines are crotonylated or acetylated depends on the relative intracellular concentrations of crotonyl-CoA and acetyl-CoA, and adding crotonate to cell cultures, or reducing the intracellular levels of acetyl-CoA, leads to an increase in histone crotonylation through the direct production of crotonyl-CoA. However, in plant the relationship of acetylation and crotonylation and the effect of the concentration of acetyl-CoA on protein crotonylation were not well known. Our previous study showed that PhACL silencing changed the content of acetyl CoA in petunia corollas. In this study, we performed a global crotonylation proteome analysis of petunia (Petunia hybrida) and found that protein crotonylation have close relationship with protein acetylation and the protein with more crotonylation sites often had more acetylation sites. Crotonylated proteins and acetylated proteins enriched in many common KEGG pathway. However, PhACL silencing resulted in different KEGG pathway enrichment of proteins with different level of crotonylated sites and acetylated sites. Cytoplasm non-histone lysine crotonylation may not depend on the concentrations of acetyl-CoA in petunia corollas. There was a positive correlation between crotonylome and acetylome expression levels in corollas of PhACL-silenced plants and control.

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