ArticleMolecular cell2026
H4K16 acylations destabilize chromatin architecture and facilitate transcriptional response during metabolic perturbations.
Article in Molecular cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Propionic acidemia as a framework for understanding the impact of disturbed propionyl-CoA on histone modifications.Biochemical Society transactions · 2026Review
- Simulating Dilute-Solution Properties and Behavior of Flexible Macromolecules: A Review of Brownian Dynamics, Monte Carlo Methods, and Computational Tools (SIMUFLEX and MONTEHYDRO) with Applications to Biomacromolecules and Selected Synthetic Polymers.International journal of molecular sciences · 2026Review
- The impact of microbial metabolites on host chromatin and epigenetic regulation.Nature metabolism · 2026Review
- UFL1-Mediated UFMylation of ENO1 Restrains Aerobic Glycolysis and Colorectal Cancer Progression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Free energy spectroscopy reveals the mechanistic landscape of chromatin compaction.Nucleic acids research · 2026Article
- Acetyl-CoA Synthetase 1 regulates global histone propionylation and metabolic stress responses.bioRxiv : the preprint server for biology · 2026Article
- Lysine Propionylation as a Metabolically Coupled PTM: Mechanisms, Functional Consequences, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
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Authors and funding
20 authors.
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Abstract
Histone modifications play crucial roles in genome function. However, how chromatin integrates physiological and metabolic responses at the molecular level remains largely unknown. Acetylation of histone H4 lysine 16 (H4K16ac) is unique, as it directly regulates chromatin architecture. Here, we investigated the roles of two additional H4K16 short-chain acylations, propionylation (H4K16pr) and butyrylation (H4K16bu), in chromatin architecture and transcriptional regulation. We demonstrate distinct in vitro effects of H4K16 acylations on chromatin structure, including inter- and intra-nucleosomal interactions. Utilizing a mouse model of the metabolic disease propionic acidemia, we reveal a transcriptional response concomitant with changes in H4K16 acylations in vivo. Our work suggests the importance of simultaneous action of histone acylations for transcriptional robustness through effects on nucleosomal interactions. We propose that this mode of action distinguishes H4K16 acylations from other modifications that also differ by one carbon, such as methylations.
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