关于举行“Modify the Modifier, a Convoluted Tale of Ubiquitin”学术报告的通知

时间:2019-07-11    点击数:

报告时间:2019年7月15日(星期一) 上午10:00

报告地点:能源基础楼一楼会议室

报告人:唐淳 研究员,中国科学院武汉物理与数学研究所

  报告摘要:

  Ubiquitin (Ub) has served as a model system in NMR for many years. Though only having 76 residues, Ub has rich dynamics in ps-ns and ns-μs timescales, allowing Ub to interact with its myriad binding partners. Ub itself has important biological functions. Catalyzed by a cascade of enzymes, Ub can be covalently attached to substrate proteins, a post-translational modification known as ubiquitylation. Moreover, multiple Ub molecules can be covalently linked to make polyubiquitin (polyUb). My group has previously shown that Ub molecules can noncovalently and dynamically interact with each other with millimolar KD, while the interactions become restricted by the covalent Ub linkage, resulting in a distinct conformational space. Using paramagnetic NMR and other techniques, we have characterized the dynamic ensemble structures of K48-linked and K63-linked di-ubiquitins. I will also present that, while Ub modifies its substrate protein, the substrate protein, in return, also affects the structural dynamics of Ub. Ub can also be phosphorylated by kinase PINK1, and the phosphorylated Ub (pUb) is involved in mitophagy and other important cellular processes. I will present that, pUb undergoes ms-s timescale dynamics, which is hardly visualized for the unmodified Ub. Moreover, I will show that, the phosphorylation makes Ub a pH sensor, as both phosphorylated Ub monomer and polyUb can alternate among different conformational states in response to subtle pH change. In addition, I will present the integrative use of chemical cross-linking and single-molecule FRET for the depiction of protein dynamics.

  报告人简介:

  唐淳研究员。中科院核心骨干特聘研究员、武汉光电国家研究中心兼聘教授,担任中科院生物磁共振分析重点实验室主任。唐淳研究员是基金委杰出青年基金获得者,中组部万人计划“青年拔尖人才”和美国霍华德休斯医学研究所(HHMI)国际青年科学家;入选国家级百千万人才工程被授予“有突出贡献中青年科学家”,入选科技部创新人才推进计划“中青年科技创新领军人才”,入选科技部首批“科技创新创业辅导师”,任中国生物物理学会生物磁共振分会理事长、湖北省晶体学会理事长、中国生物物理学会理事等职。唐淳研究员长期从事生物磁共振及整合计算生物学中的方法学研究,重点关注蛋白质、RNA等生物大分子在执行生物学功能的过程中其空间构象如何动态变化。已发表论文50 余篇,以第一或通讯作者在NatureNature子刊、PNASJACSAngew Chem 等发表论文多篇,累计引用近3000次。

  联系人:1810组 张丽华 研究员

  联系电话:84379720


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