报告题目：Biochemical mechanisms of NLR signaling in plants
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) .
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.