Ziping Niu, Chen Chen, Siyu Wang, Congcong Lu, Zhiyue Wu, Aiyuan Wang, Jing Mo, Jianji Zhang, Yanpu Han, Ye Yuan, Yingao Zhang, Yong Zang, Chaoran He, Xue Bai, Shanshan Tian, Guijin Zhai, Xudong Wu, Kai Zhang
Lysine lactylation (Kla) links metabolism and gene regulation and plays a key role in multiple biological processes. However, the regulatory mechanism and functional consequence of Kla remain to be explored. Here, we report that HBO1 functions as a lysine lactyltransferase to regulate transcription. We show that HBO1 catalyzes the addition of Kla in vitro and intracellularly, and E508 is a key site for the lactyltransferase activity of HBO1. Quantitative proteomic analysis further reveals 95 endogenous Kla sites targeted by HBO1, with the majority located on histones...
April 26, 2024: Nature Communications