Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1  

作　　者：Jiao Tang Zhifu Han Yadong Sun Heqiao Zhang Xinqi Gong Jijie Chai 

机构地区：[1]Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China

出　　处：《Cell Research》2015年第1期110-120,共11页细胞研究（英文版）

基　　金：We thank Yu F and He J at Shanghai Synchrotron Radiation Facility （SSRF）. The research was funded by the National Natural Science Foundation of China （31420103906 and 31130063）, the Chinese Ministry of Science and Technology （2014CB910101） and the National Outstanding Young Scholar Science Foundation of China （31025008 to JC）.

摘　　要：The endogenous peptides AtPepl-8 in Arabidopsis mature from the conserved C-terminal portions of their precursor proteins PROPEP1-8, respectively. The two homologous leucine-rich repeat-receptor kinases （LRR-RKs） PEPR1 and PEPR2 act as receptors of AtPeps. AtPep binding leads to stable association of PEPR1,2 with the shared receptor LRR-RK BAK1, eliciting immune responses similar to those induced by pathogens. Here we report a crystal structure of the extraceUular LRR domain of PEPRI （PEPR1LRR） in complex with AtPepl. The structure reveals that AtPepl adopts a fully extended conformation and binds to the inner surface of the superhelical PEPRILRR. Biochemical assays showed that AtPepl is capable of inducing PEPR1LRR-BAK1LRR heterodimerization. The conserved C-terminal portion of AtPepl dominates AtPepl binding to PEPRILRR, with the last amino acid of AtPepl Asn23 forming extensive interactions with PEPR1LRR. Deletion of the last residue of AtPepl significantly compromised AtPep1 interaction with PEPRILRR. Together, our data reveal a conserved structural mechanism of AtPep1 recognition by PEPR1, providing significant insight into prediction of recognition of other peptides by their cognate LRR-RKs.

关 键 词：PEPR1 LRR AtPeps BAK1 repeat-receptor kinase crystal structure 

分 类 号：Q58[生物学—生物化学] S635.036[农业科学—蔬菜学]