To Nibble at Plant Resistance Proteins

被引：131

作者：

Takken, F. L. W. ^{[1
]}

Tameling, W. I. L. ^{[2
]}

机构：

[1] Univ Amsterdam, SILS, NL-1090 GE Amsterdam, Netherlands

[2] Wageningen Univ, Phytopathol Lab, NL-6700 EE Wageningen, Netherlands

来源：

SCIENCE | 2009年 / 324卷 / 5928期

关键词：

NB-LRR PROTEIN; NUCLEOTIDE-BINDING; CASPASE-1; ACTIVATION; ATP HYDROLYSIS; APOPTOSOME; RECOGNITION; PERCEPTION; MUTATIONS; EXCHANGE; DOMAINS;

D O I：

10.1126/science.1171666

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：

To intercept invading microbes that threaten growth and reproduction, plants evolved a sophisticated innate immune system. Recognition of specialized pathogens is mediated by resistance proteins that function as molecular switches. Pathogen perception by these multidomain proteins seems to trigger a series of conformational changes dependent on nucleotide exchange. The activated resistance protein switches on host defenses, often culminating in the death of infected cells. Given their control over life and death, activity of these proteins requires tight regulation that involves intramolecular interactions between the various domains.

引用

页码：744 / 746

页数：3

共 27 条

[11] STANDing strong, resistance proteins instigators of plant defence [J].

Lukasik, Ewa ;

Takken, Frank L. W. .

CURRENT OPINION IN PLANT BIOLOGY, 2009, 12 (04) :427-436

[12] Inflammasome adaptors and sensors: intracellular regulators of infection and inflammation [J].

Mariathasan, Sanjeev ;

Monack, Denise M. .

NATURE REVIEWS IMMUNOLOGY, 2007, 7 (01) :31-40

[13] How integration of positive and negative regulatory signals by a STAND signaling protein depends on ATP hydrolysis [J].

Marquenet, Emelie ;

Richet, Evelyne .

MOLECULAR CELL, 2007, 28 (02) :187-199

[14] Elicitor-mediated oligomerization of the tobacco N disease resistance protein [J].

Mestre, P ;

Baulcombe, DC .

PLANT CELL, 2006, 18 (02) :491-501

[15] NRG1, a CC-NB-LRR protein, together with N, a TIR-NB-LRR protein, mediates resistance against tobacco mosaic virus [J].

Peart, JR ;

Mestre, P ;

Lu, R ;

Malcuit, I ;

Baulcombe, DC .

CURRENT BIOLOGY, 2005, 15 (10) :968-973

[16] Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHT-LRR proteins [J].

Rairdan, Greg ;

Moffett, Peter .

MICROBES AND INFECTION, 2007, 9 (05) :677-686

[17] The coiled-coil and nucleotide binding domains of the potato Rx disease resistance protein function in pathogen recognition and signaling [J].

Rairdan, Gregory J. ;

Collier, Sarah M. ;

Sacco, Melanie A. ;

Baldwin, Thomas T. ;

Boettrich, Teresa ;

Moffett, Peter .

PLANT CELL, 2008, 20 (03) :739-751

[18] Distinct domains in the ARC region of the potato resistance protein Rx mediate LRR binding and inhibition of activation [J].

Rairdan, Gregory J. ;

Moffett, Peter .

PLANT CELL, 2006, 18 (08) :2082-2093

[19] Structure of the apoptotic protease-activating factor 1 bound to ADP [J].

Riedl, SJ ;

Li, WY ;

Chao, Y ;

Schwarzenbacher, R ;

Shi, YG .

NATURE, 2005, 434 (7035) :926-933

[20] The apoptosome: signalling platform of cell death [J].

Riedl, Stefan J. ;

Salvesen, Guy S. .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2007, 8 (05) :405-413

← 1 2 3 →