Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein

被引:318
作者
Hubert, DA
Tornero, P
Belkhadir, Y
Krishna, P
Takahashi, A
Shirasu, K
Dangl, JL
机构
[1] Univ N Carolina, Dept Biol, Chapel Hill, NC 27599 USA
[2] Univ N Carolina, Curriculum Genet, Chapel Hill, NC 27599 USA
[3] Univ N Carolina, Dept Microbiol & Immunol, Chapel Hill, NC 27599 USA
[4] Univ Western Ontario, Dept Biol, London, ON N6A 5B7, Canada
[5] John Innes Ctr Plant Sci Res, Sainsbury Lab, Norwich NR4 7UH, Norfolk, England
关键词
HSP90; plant disease; RAR1; RPM1; SGT1; HEAT-SHOCK-PROTEIN; PLASMA-MEMBRANE; BINDING SITE; ATP BINDING; GENE; THALIANA; RAR1; IDENTIFICATION; RECOGNITION; INTERACTS;
D O I
10.1093/emboj/cdg547
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Arabidopsis protein RPM1 activates disease resistance in response to Pseudomonas syringae proteins targeted to the inside of the host cell via the bacterial type III delivery system. We demonstrate that specific mutations in the ATP-binding domain of a single Arabidopsis cytosolic HSP90 isoform compromise RPM1 function. These mutations do not affect the function of related disease resistance proteins. RPM1 associates with HSP90 in plant cells. The Arabidopsis proteins RAR1 and SGT1 are required for the action of many R proteins, and display some structural similarity to HSP90 co-chaperones. Each associates with HSP90 in plant cells. Our data suggest that (i) RPM1 is an HSP90 client protein; and (ii) RAR1 and SGT1 may function independently as HSP90 cofactors. Dynamic interactions among these proteins can regulate RPM1 stability and function, perhaps similarly to the formation and regulation of animal steroid receptor complexes.
引用
收藏
页码:5679 / 5689
页数:11
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