Mengqing Gao, Jin Wang, Sophie Rousseaux, Minjia Tan, Lulu Pan, Lijun Peng, Sisi Wang, Wenqian Xu, Jiayi Ren, Yuanfang Liu, Martin Spinck, Sophie Barral, Tao Wang, Florent Chuffart, Ekaterina Bourova-Flin, Denis Puthier, Sandrine Curtet, Lisa Bargier, Zhongyi Cheng, Heinz Neumann, Jian Li, Yingming Zhao, Jian-Qing Mi, Saadi Khochbin
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' specific roles. Here, by using an acute lymphoblastic leukemia (ALL) cell model and blasts from individuals with B-precusor ALL (B-ALL), we demonstrate a role of mitochondrial activity in controlling the histone acylation/acetylation ratio, especially at histone H4 lysine 5 (H4K5)...
July 27, 2021: Cell Reports