Structural insights into activation mechanisms on NADase of the bacterial DSR2 anti-phage defense system
文献类型： 外文期刊
作者： Zhang, Hong 1 ; Li, Yu 3 ; Li, Lanlan 1 ; Chen, Lifei 1 ; Zhu, Chunhua 5 ; Sun, Lifang 1 ; Dong, Panpan 1 ; Jing, Dingding 1 ; Yang, Jinbo 1 ; Fu, Lei 1 ; Xiao, Fangnan 1 ; Xia, Ningshao 3 ; Li, Shaowei 3 ; Zheng, Qingbing 3 ; Wu, Yunkun 1 ;
作者机构： 1.Fujian Normal Univ, Coll Life Sci, Prov Univ Key Lab Cellular Stress Response & Metab, Fuzhou 350117, Peoples R China
2.Fujian Normal Univ, Coll Life Sci, Fujian Key Lab Dev & Neural Biol, Fuzhou 350117, Peoples R China
3.Xiamen Univ, Sch Life Sci, Sch Publ Hlth, State Key Lab Vaccines Infect Dis,Xiang An Biomed, Xiamen 361102, Peoples R China
4.Xiamen Univ, Natl Inst Diagnost & Vaccine Dev Infect Dis, Collaborat Innovat Ctr Biol Prod, Natl Innovat Platform Ind Educ Integrat Vaccine Re, Xiamen 361102, Peoples R China
5.Fujian Acad Agr Sci, Inst Anim Husb & Vet Med, Fuzhou 350013, Peoples R China
期刊名称：SCIENCE ADVANCES （ 影响因子：11.7； 五年影响因子：13.7 ）
ISSN： 2375-2548
年卷期： 2024 年 10 卷 31 期
页码：
收录情况： SCI
摘要： As a sirtuin (SIR2) family protein, defense-associated sirtuin2 (DSR2) has been demonstrated to participate in bacterial anti-phage resistance via depleting nicotinamide adenine dinucleotide (NAD+) of infected cells, which can be activated by tail tube protein (TTP) and inhibited by DSR anti-defense 1 (DSAD1) of diverse phages. However, the regulating mechanism remains elusive. Here, we determined the cryo-electron microscopy structure of apo DSR2, as well as the respective complex structures with TTP and DSAD1. Structural analyses and biochemical studies reveal that DSR2 forms a tetramer with a SIR2 central core and two distinct conformations. Monomeric TTP preferentially binds to the closed conformation of DSR2, inducing conformational distortions on SIR2 tetramer assembly to activate its NADase activity. DSAD1 combines with the open conformation of DSR2, directly or allosterically inhibiting TTP activation on DSR2 NAD+ hydrolysis. Our findings decipher the detailed molecule mechanisms for DSR2 NADase activity regulation and lay a foundation for in-depth understanding of the DSR2 anti-phage defense system.
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