报告题目：Chemical Approaches to Decode Histone Epigenetics
报告人：Xiang David Li 教授 
主持人：方  东 研究员
时   间：2024年5月23日（周四）下午4点
地   点：纳米楼457报告厅
报告人简介：

Dr. Xiang David Li obtained his B.Sc. in chemistry from Fudan University in 2003, and Ph.D. in organic and bioorganic chemistry in 2008 from The University of Hong Kong under the supervision of Professor Dan Yang. He then moved to New York to conduct his postdoctoral training in chemistry and cell biology with Prof. Tarun M. Kapoor at Rockefeller University. In 2011, he returned to The University of Hong Kong to start his independent career as an assistant professor and was promoted to associate professor in 2017 and full professor in 2020. Dr. Li’s research, at the interface of chemistry and biology, focuses on developing novel chemical tools and approaches to decipher the biological significance and regulatory mechanisms of histone posttranslational modifications. Dr. Li has been recognized by multiple prizes and awards, including Tetrahedron Young Investigator Award for Bioorganic and Medicinal Chemistry, CAPA Distinguished Faculty Award, NSFC Excellent Young Scientists Award, and Early Career Award from the Hong Kong Research Grant Council.

讲座摘要：

Histone posttranslational modifications (PTMs), such as phosphorylation, methylation and acetylation, play crucial roles in regulating many fundamental cellular processes, such as gene transcription, DNA replication, DNA damage repair, chromosome segregation, and cell differentiation. Increasing evidence has indicated that PTMs of histones can serve as a heritable ‘code’ (so-called ‘histone code’), which provides epigenetic information that a mother cell can pass to its daughters. Histone code is ‘written’ or ‘erased’ by enzymes that generate or remove the modifications of histones. Meanwhile, ‘readers’ of histone code recognize specific histone modifications and ‘translate’ the code by executing distinct cellular programs necessary to establish the diverse cell phenotypes.

While a large number of PTMs have been identified on histones, the biological significance of vast majority of them remains poorly understood. This is particularly the case for those newly discovered histone modifications such as lysine crotonylation, succinylation, fatty-acid acylation, and the modifications present at histone cores such as methylation at H3 lysine 79. Studies of these new PTMs are hindered by the lack of knowledge about their regulating enzymes (i.e., ‘writers’ and ‘erasers’) and functional binding proteins (i.e., ‘readers’). To fill this knowledge gap, here I present the development of novel chemical tools and approaches, in combination with the state-of-the-art biochemistry, proteomics and cell biology methods, to comprehensively identify ‘writers’, ‘erasers’ and ‘readers’ of histone PTMs and examine their regulatory mechanisms and cellular functions.