The structural basis for activation of plant immunity by bacterial effector protein AvrPto

被引:143
作者
Xing, Weiman
Zou, Yan
Liu, Qun
Liu, Jianing
Luo, Xi
Huang, Qingqiu
Chen, She
Zhu, Lihuang
Bi, Ruchang
Hao, Quan
Wu, Jia-Wei
Zhou, Jian-Min
Chai, Jijie
机构
[1] Natl Inst Biol Sci, Beijing 102206, Peoples R China
[2] Tsinghua Univ, Dept Biol Sci & Biotechnol, Beijing 100084, Peoples R China
[3] Cornell Univ, Cornell High Energy Synchrotron Source, Ithaca, NY 14853 USA
[4] Chinese Acad Sci, Inst Genet & Dev Biol, Beijing 100101, Peoples R China
[5] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
关键词
D O I
10.1038/nature06109
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Pathogenic microbes use effectors to enhance susceptibility in host plants. However, plants have evolved a sophisticated immune system to detect these effectors using cognate disease resistance proteins(1), a recognition that is highly specific, often elicits rapid and localized cell death, known as a hypersensitive response, and thus potentially limits pathogen growth(2-5). Despite numerous genetic and biochemical studies on the interactions between pathogen effector proteins and plant resistance proteins, the structural bases for such interactions remain elusive. The direct interaction between the tomato protein kinase Pto and the Pseudomonas syringae effector protein AvrPto is known to trigger disease resistance and programmed cell death(6,7) through the nucleotide-binding site/leucine-rich repeat (NBS-LRR) class of disease resistance protein Prf(8). Here we present the crystal structure of an AvrPto-Pto complex. Contrary to the widely held hypothesis that AvrPto activates Pto kinase activity, our structural and biochemical analyses demonstrated that AvrPto is an inhibitor of Pto kinase in vitro. The AvrPto-Pto interaction is mediated by the phosphorylation-stabilized P+1 loop and a second loop in Pto, both of which negatively regulate the Prf-mediated defences in the absence of AvrPto in tomato plants. Together, our results show that AvrPto derepresses host defences by interacting with the two defence-inhibition loops of Pto.
引用
收藏
页码:243 / U11
页数:6
相关论文
共 29 条
[1]   Plant disease resistance protein signaling: NBS-LRR proteins and their partners [J].
Belkhadir, Y ;
Subramaniam, R ;
Dangl, JL .
CURRENT OPINION IN PLANT BIOLOGY, 2004, 7 (04) :391-399
[2]   PHOSPHOTRANSFERASE AND SUBSTRATE BINDING MECHANISM OF THE CAMP-DEPENDENT PROTEIN-KINASE CATALYTIC SUBUNIT FROM PORCINE HEART AS DEDUCED FROM THE 2.0 ANGSTROM STRUCTURE OF THE COMPLEX WITH MN2+ ADENYLYL IMIDODIPHOSPHATE AND INHIBITOR PEPTIDE PKI(5-24) [J].
BOSSEMEYER, D ;
ENGH, RA ;
KINZEL, V ;
PONSTINGL, H ;
HUBER, R .
EMBO JOURNAL, 1993, 12 (03) :849-859
[3]   Functional analyses of the Pto resistance gene family in tomato and the identification of a minor resistance determinant in a susceptible haplotype [J].
Chang, JH ;
Tai, YS ;
Bernal, AJ ;
Lavelle, DT ;
Staskawicz, BJ ;
Michelmore, RW .
MOLECULAR PLANT-MICROBE INTERACTIONS, 2002, 15 (03) :281-291
[4]   Host-microbe interactions: Shaping the evolution of the plant immune response [J].
Chisholm, ST ;
Coaker, G ;
Day, B ;
Staskawicz, BJ .
CELL, 2006, 124 (04) :803-814
[5]   CURRENT STATUS OF GENE-FOR-GENE CONCEPT [J].
FLOR, HH .
ANNUAL REVIEW OF PHYTOPATHOLOGY, 1971, 9 :275-+
[6]   Recognition specificity for the bacterial avirulence protein AvrPto is determined by Thr-204 in the activation loop of the tomato Pto kinase [J].
Frederick, RD ;
Thilmony, RL ;
Sessa, G ;
Martin, GB .
MOLECULAR CELL, 1998, 2 (02) :241-245
[7]   Salmonella interactions with host cells:: Type III secretion at work [J].
Galán, JE .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 2001, 17 :53-86
[8]  
He P, 2006, CELL, V125, P563, DOI 10.1016/j.cell.2006.02.047
[9]   Type III protein secretion mechanism in mammalian and plant pathogens [J].
He, SY ;
Nomura, K ;
Whittam, TS .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2004, 1694 (1-3) :181-206
[10]   Type III protein secretion systems in bacterial pathogens of animals and plants [J].
Hueck, CJ .
MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 1998, 62 (02) :379-+