Molecular Mechanisms of the Interactions of the CoREST Complex and Chromatin
发布时间 :2021-06-22  阅读次数 :17600

报告人:Mingxuan Wu(吴明轩博士)

School of Science, Westlake University, Hangzhou





Chromatin remodeling and histone modifications play essential roles in the regulation of gene activation or silencing in physiologic and disease processes. The CoREST complex can deacetylate and demethylate modified histones in chromatin but the interplay between the subunits of this complex and their interactions with nucleosomes is largely unknown. We use engineered sortase to generate histone H3 containing post-translational modifications (PTMs) that ligates H3 N-tail depsipeptides and globular histone H3 with excellent conversions. Next, we prepared a group of nucleosome substrates containing H3K4-dimethyl and assorted H3 acetyl-Lys modifications as well as nucleosome tools containing N-propargyl and hydroxamic acid functionalities. Using a purified core CoREST complex, we explored its enzymatic features in processing modified H3 N-tail peptides and nucleosomes. In addition, the novel private non-profit research-oriented university, Westlake University, will be briefly introduced as well as the career opportunities for students and postdocs.


Speaker biography

Mingxuan grew up in Zhengzhou and went to the School of Life Science and Biotechnology at Shanghai Jiao Tong University in 2004 for a 6 year B.S.-M.S. program (基地班). Mingxuan then moved to the Garden State in the U.S. and graduated from Princeton University with chemistry Ph.D. in 2015. Next he went to Maryland, where he joined the Phil Cole lab for postdoc training at Johns Hopkins University School of Medicine, and later moved to Harvard Medical School Brigham and Women’s Hospital in 2017. Mingxuan joined the School of Science at Westlake University in fall 2019 as an assistant professor. His research interests include developments of novel chemical tools to understand how chromatin remodeling complexes regulate gene transcription via histone modifications.