Metabolically controlled histone H4K5 acylation/acetylation ratio drives BRD4 genomic distribution

• Published in: Cell reports (Cambridge) Vol. 36; no. 4; p. 109460
• Main Authors: Gao, Mengqing, Wang, Jin, Rousseaux, Sophie, Tan, Minjia, Pan, Lulu, Peng, Lijun, Wang, Sisi, Xu, Wenqian, Ren, Jiayi, Liu, Yuanfang, Spinck, Martin, Barral, Sophie, Wang, Tao, Chuffart, Florent, Bourova-Flin, Ekaterina, Puthier, Denis, Curtet, Sandrine, Bargier, Lisa, Cheng, Zhongyi, Neumann, Heinz, Li, Jian, Zhao, Yingming, Mi, Jian-Qing, Khochbin, Saadi
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 27.07.2021; Elsevier
• Subjects: Acetylation; Acylation; Biochemistry, Molecular Biology; Cell Cycle Proteins - metabolism; Cell Line, Tumor; Chromatin - metabolism; Fatty Acids - biosynthesis; Female; Gene Expression Regulation, Leukemic; Genome, Human; Genomics; Histones - metabolism; Humans; Life Sciences; Lysine - metabolism; Mitochondria - metabolism; Mitochondrial Proteins - metabolism; Models, Biological; Oxidation-Reduction; Precursor Cell Lymphoblastic Leukemia-Lymphoma - genetics; Precursor Cell Lymphoblastic Leukemia-Lymphoma - pathology; Protein Binding; Protein Processing, Post-Translational; RNA-Binding Proteins - metabolism; Transcription Factors - metabolism

In addition to acetylation, histones are modified by a series of competing longer-chain acylations. Most of these acylation marks are enriched and co-exist with acetylation on active gene regulatory elements. Their seemingly redundant functions hinder our understanding of histone acylations’ specifi...