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(2017年09月07日) 报告人:Yujun George Zheng (University of Georgia)
发表时间:2017-09-01 阅读次数:261次

报告题目: Chemical Biology of Protein Lysine Acetylation

报告人: Yujun George Zheng. Associate Professor, Graduate Coordinator, Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, University of Georgia.

报告时间:2017年09月07日(星期四) 10:00-12:00AM

报告地点:同济大学 化学馆120室

 

报告人简介:

Education:

1990-1995 B.S., Chemistry, Department of Chemistry, Peking University, Beijing, China

1995-1998 M.S., Chemistry, Department of Chemistry, Peking University, Beijing, China

1998-2002 Ph.D., Chemistry, Department of Chemistry, University of Miami, Florida

Awards and Honors:

1. Co-Founder and Co-Organizer, Southeastern Chemical Biology Symposium – April 2017

2. Provost's list of UGA “Super Research Stars”, 2015

3. Leading Organizer, Pacifichem – Symposium on Epigenetic and Chromatin Biochemistry,            

  Dec 2015

4. “Most Productive Faculty” in Department of Pharmaceutical and Biomedical Sciences.  Summer 2014

Editorial Board Membership:

2009 - present Editorial board member, BioMed Research International.

2015 - present Scientific advisor board member, Chrysalis Therapeutics, Inc.

 

报告摘要:Dynamic lysine acetylation of proteins is involved in a variety of fundamental biological processes including epigenetic programing, cell cycle, apoptosis, metabolism, and signal transduction. Acetylation is introduced by protein lysine acetyltransferases (KATs) which transfer the acetyl group from the co-substrate acetyl-coenzyme A (acetyl-CoA, Ac-CoA) to the epsilon-amino group of specific lysine residues in proteins. Elucidating biological and pathological functions of protein lysine acetyltransferases (KATs) greatly depends on the knowledge of the dynamic and spatial localization of their enzymatic targets in the cellular proteome. We report the design and application of chemical probes for facile labeling and detection of substrates of the three major human KAT enzymes. In this approach, a series of acetyl-CoA analogs with functional groups were synthesized for selective labeling and detection of KAT substrates. Meanwhile, we replaced the bulky residues in the cofactor-binding site of several KATs with smaller residues by site-directed mutagenesis in order to expand the cofactor binding pocket for AcCoA derivatives. Rationally designed KAT-cofactor pairs are applied in conjunction with “clickable” reporters for KAT substrate labeling. The functionalized and transferable acyl moiety of the Ac-CoA analogs further allowed the labeled substrates to be probed with alkynyl or azido-tagged fluorescent reporters by the copper-catalyzed azide−alkyne cycloaddition. The AcCoA analogs in combination with the rational protein-engineering approach provide powerful molecular tools for labeling and mapping KAT targets in the context of complex

biological mixtures at the proteomic level.

 

 

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