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学术报告

【学术交流会】微生物代谢国家重点实验室学术交流会2018-[03]

主要完成人: 发表日期:2018-03-01 点击数:667

微生物代谢国家重点实验室学术交流会 暨国重实验室科技创新训练课程

SKLMM Workshop

2018-[03]

      Presentation in Chinese

报告题目:Ubiquitination lessons taught by a bacterial pathogen

报告人简介:

罗招庆,国家“千人计划”特聘教授。2001年获美国伊利诺依大学厄巴那-香槟分校博士学位。2001-2004年在美国塔夫茨大学医学院做博士后研究。2004年起就职于普渡大学,历任助理教授,副教授,教授。2017年-至今,吉林大学第一医院。

报告摘要:

Classical ubiquitination is catalyzed by the action of E1, E2 and E3 enzymes that function coordinately to covalently link the modifier to protein substrates. We recently found that members of the SidE effector family from the bacterial pathogen Legionella pneumophila, such as SdeA catalyze ubiquitination in a mechanism that completely differs from the canonical three-enzyme cascade. In this scenario, the reaction deoes not require ATP, instead, ubiquitin is activated by ADP-ribosylation at Arg42 (ADPR-Ub) via a mono-ADP-ribosyltransferase (mART) motif. Subsequent works by others showed that this reaction intermediate is utilized by a phosphodiesterase (PDE) activity also embedded in SdeA, which cleaves ADPR-Ub and transfers the phosphoribosylated ubiquitin moiety to serine residues of target proteins accompanied by the release of the AMP moiety. In our efforts to investigate potential eukaryotic enzymes capable of catalyzing ubiquitination by similar mechanism, we found that a L. pneumophila effector ubiquitinates an E2 enzyme in the host cell by a novel single-step reaction, leading to the inhibition of its activity. In this presentation, I will discuss the mechanisms of these modifications and their implications in cell signaling during L. pneumophila infection.

  间:    20180307日星期三上午09:30-10:30

  点:    闵行校区生物药学楼树华多功能厅(800号)

主持人:    许平 教授

欢迎广大师生参加!

微生物代谢国家重点实验室

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