Structural and functional analysis of SGT1-HSP90 core complex required for innate immunity in plants

被引：48

作者：

Kadota, Yasuhiro ^{[3
]}

Amigues, Beatrice ^{[1
,2
]}

Ducassou, Lionel ^{[1
,2
]}

Madaoui, Hocine ^{[1
,2
]}

Ochsenbein, Francoise ^{[1
,2
]}

Guerois, Raphael ^{[1
,2
]}

Shirasu, Ken ^{[3
]}

机构：

[1] IBITECS, CEA, Gif Sur Yvette, France

[2] CNRS, Gif Sur Yvette, France

[3] RIKEN, Plant Sci Ctr, Tsurumi Ku, Yokohama, Kanagawa, Japan

来源：

EMBO REPORTS | 2008年 / 9卷 / 12期

基金：

日本学术振兴会;

关键词：

molecular chaperone; co-chaperone; disease resistance; resistance protein;

D O I：

10.1038/embor.2008.185

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：

SGT1 (Suppressor of G2 allele of skp1), a co-chaperone of HSP90 (Heat-shock protein 90), is required for innate immunity in plants and animals. Unveiling the cross talks between SGT1 and other co-chaperones such as p23, AHA1 (Activator of HSP90 ATPase 1) or RAR1 (Required for MIa12 resistance) is an important step towards understanding the HSP90 machinery. Nuclear magnetic resonance spectroscopy and mutational analyses of HSP90 revealed the nature of its binding with the CS domain of SGT1. Although CS is structurally similar to p23, these domains were found to non-competitively bind to various regions of HSP90; yet, unexpectedly, full- length SGT1 could displace p23 from HSP90. RAR1 partly shares the same binding site with HSP90 as the CS domain, whereas AHA1 does not. This analysis allowed us to build a structural model of the HSP90-SGT1 complex and to obtain a compensatory mutant pair between both partners that is able to restore virus resistance in vivo through Rx (Resistance to potato virus X) immune sensor stabilization.

引用

页码：1209 / 1215

页数：7

共 19 条

[1] Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex [J].