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Histone acylation marks respond to metabolic perturbations and enable cellular adaptation

Title
Histone acylation marks respond to metabolic perturbations and enable cellular adaptation
Authors
Jo, ChanheePark, SeokjaeOh, SungjoonChoi, JinmiKim, Eun-KyoungYoun, Hong-DukCho, Eun-Jung
DGIST Authors
Jo, Chanhee; Park, Seokjae; Oh, Sungjoon; Choi, Jinmi; Kim, Eun-Kyoung; Youn, Hong-Duk; Cho, Eun-Jung
Issue Date
2020-12
Citation
Experimental and Molecular Medicine, 52, 2005-2019
Type
Article
Article Type
Article
Keywords
ACETYL-COAACYL-COASKELETAL-MUSCLEGENE-EXPRESSIONCROTONYLATIONDIFFERENTIATIONPROPIONYLATIONIDENTIFICATIONPROLIFERATIONTRANSCRIPTION
ISSN
1226-3613
Abstract
Acetylation is the most studied histone acyl modification and has been recognized as a fundamental player in metabolic gene regulation, whereas other short-chain acyl modifications have only been recently identified, and little is known about their dynamics or molecular functions at the intersection of metabolism and epigenetic gene regulation. In this study, we aimed to understand the link between nonacetyl histone acyl modification, metabolic transcriptional regulation, and cellular adaptation. Using antibodies specific for butyrylated, propionylated, and crotonylated H3K23, we analyzed dynamic changes of H3K23 acylation upon various metabolic challenges. Here, we show that H3K23 modifications were highly responsive and reversibly regulated by nutrient availability. These modifications were commonly downregulated by the depletion of glucose and recovered based on glucose or fatty acid availability. Depletion of metabolic enzymes, namely, ATP citrate lyase, carnitine acetyltransferase, and acetyl-CoA synthetase, which are involved in Ac-CoA synthesis, resulted in global loss of H3K23 butyrylation, crotonylation, propionylation, and acetylation, with a profound impact on gene expression and cellular metabolic states. Our data indicate that Ac-CoA/CoA and central metabolic inputs are important for the maintenance of histone acylation. Additionally, genome-wide analysis revealed that acyl modifications are associated with gene activation. Our study shows that histone acylation acts as an immediate and reversible metabolic sensor enabling cellular adaptation to metabolic stress by reprogramming gene expression. © 2020, The Author(s).
URI
http://hdl.handle.net/20.500.11750/12658
DOI
10.1038/s12276-020-00539-x
Publisher
Springer Nature
Related Researcher
  • Author Kim, Eun-Kyoung Lab of Neuro-Metabolism & Neurometabolomic Research Center
  • Research Interests Neural functions in metabolic diseases; 뇌신경세포와 비만; 당뇨 등의 대사 질환 관련 연구
Files:
Collection:
Department of Brain and Cognitive SciencesLab of Neuro-Metabolism & Neurometabolomic Research Center1. Journal Articles


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