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EMBO reports 9, 12, 1209–1215 (2008)
doi:10.1038/embor.2008.185
AOP Published online: 3 October 2008
Structural and functional analysis of SGT1–HSP90 core complex required for innate immunity in plants
EMBO Open
Yasuhiro Kadota1, Beatrice Amigues2, Lionel Ducassou2, Hocine Madaoui2, Francoise Ochsenbein2, Raphaël Guerois2 & Ken Shirasu1
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1 RIKEN Plant Science Center, Suehiro-cho 1-7-22 Tsurumi-ku, Yokohama, Japan
2 CEA, Institut de Biologie et Technologies de Saclay (IBITECS) and CNRS, Gif-sur-Yvette, France
To whom correspondence should be addressed
Raphaël Guerois Tel: +33 1 69 08 67 17; Fax: +33 1 69 08 92 75; E-mail: raphael.guerois@cea.fr
Ken Shirasu Tel: +81 45 503 9574; Fax: +81 45 503 9573; E-mail: ken.shirasu@psc.riken.jp
Received 14 April 2008; Accepted 26 August 2008; Published online 3 October 2008.
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Abstract
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 Mla12 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.
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