【科学家讲坛】德国洪堡教席奖获得者柴继杰教授学术报告会

2022年8月23日 上午9:00

发布者:张宁发布时间:2022-08-20浏览次数:41

应学校“科学家讲坛”邀请,德国洪堡教席奖获得者、国家杰出青年基金获得者、973项目首席科学家——柴继杰教授来amjs澳金沙官网访问,并为amjs澳金沙官网师生带来精彩学术报告,欢迎全校师生参加。

报告人:柴继杰教授

报告题目:Biochemical mechanisms of NLR signaling in plants

报告时间:2022823日(周二)上午9:0012:00

报告地点:活动中心214

主办单位:人事处

承办单位:amjs澳金沙门欢迎您、生命科学中心

报告人简介

Jijie Chai completed his PhD study in Peking Union Medical College in 1997, and conducted his postdoctoral research in Princeton University from 1999 to 2004. He joined National Institute Biological Sciences (NIBS) in 2004 to establish an independent laboratory there. After promoted from an assistance to an associate investigator in 2009, he moved to Tsinghua University. In 2017, he made a second move to join University of Cologne in Germany as an Alexander von Humboldt Professor/W3 Professor. Jijie Chai received the Alexander von Humboldt Professorship Award (Alexander von Humboldt, Foundation, Germany) in 2017. He is Max Planck Fellow at Max Planck Institute. Jijie is also a recipient of the 2020 Chinese Academy of Sciences Outstanding Scientific and Technological Achievement Award (together with Prof. Jianmin Zhou from the Chinese Academy of Sciences), the National Natural Science Award Second Prize (2017), the first prize of Henan Province Science and Technology Progress Award (2016, together with Prof. Junbiao Chang from Zhenzhou University), Chief Scientist of the Major Scientific Research Project of the Ministry of Science and Technology from 2015 to 2019, Tan Jiazhen Life Science Innovation Award (2011) and National Outstanding Youth Fund (2010) .

报告摘要

Nucleotide binding and leucine-rich repeat (NLR) containing proteins are a large family of intracellular immune receptors conserved in both animals and plants. Plant NLRs mediate specific recognition of pathogen effectors, inducing effector-triggered immunity (ETI). Direct or indirect effector recognition leads to oligomeric assemblies of plant NLRs termed resistosomes that mediate ETI immune signaling. NLR resistosomes can function as calcium-permeable channels or NADase holoenzymes. I will present our studies of resistosomes including their identifications, determination of their biochemical activities, and mechanisms of action. I will also discuss the identification of the catalytic products of resistosome holoenzymes.