Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity

Marta Boter; Beatrice Amigues; Jack Peart; Christian Breuer; Yasuhiro Kadota; Catarina Casais; Geoffrey Moore; Colin Kleanthous; Francoise Ochsenbein; Ken Shirasu; Raphael Guerois

doi:10.1105/tpc.107.050427

Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity

Marta Boter, Beatrice Amigues, Jack Peart, Christian Breuer, Yasuhiro Kadota, Catarina Casais, Geoffrey Moore, Colin Kleanthous, Francoise Ochsenbein, Ken Shirasu, Raphael Guerois

Biology

Research output: Contribution to journal › Article › peer-review

Abstract

SGT1 (for suppressor of G2 allele of skp1) and RAR1 (for required for Mla12 resistance) are highly conserved eukaryotic proteins that interact with the molecular chaperone HSP90 (for heat shock protein90). In plants, SGT1, RAR1, and HSP90 are essential for disease resistance triggered by a number of resistance (R) proteins. Here, we present structural and functional characterization of plant SGT1 proteins. Random mutagenesis of Arabidopsis thaliana SGT1b revealed that its CS (for CHORD-SGT1) and SGS (for SGT1 specific) domains are essential for disease resistance. NMR-based interaction surface mapping and mutational analyses of the CS domain showed that the CHORD II domain of RAR1 and the N-terminal domain of HSP90 interact with opposite sides of the CS domain. Functional analysis of the CS mutations indicated that the interaction between SGT1 and HSP90 is required for the accumulation of Rx, a potato (Solanum tuberosum) R protein. Biochemical reconstitution experiments suggest that RAR1 may function to enhance the SGT1-HSP90 interaction by promoting ternary complex formation.

Original language	English
Pages (from-to)	3791-3804
Number of pages	14
Journal	The Plant Cell
Volume	19
Issue number	11
DOIs	https://doi.org/10.1105/tpc.107.050427
Publication status	Published - Nov 2007

Keywords

DISEASE RESISTANCE PROTEIN
ATPASE ACTIVITY
CO-CHAPERONE
ESSENTIAL COMPONENT
CYTOSOLIC HSP90
CYSTEINE-RICH
RAR1
ARABIDOPSIS
COMPLEX
CONTRIBUTES

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10.1105/tpc.107.050427

Cite this

Boter, M., Amigues, B., Peart, J., Breuer, C., Kadota, Y., Casais, C., Moore, G., Kleanthous, C., Ochsenbein, F., Shirasu, K., & Guerois, R. (2007). Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity. The Plant Cell, 19(11), 3791-3804. https://doi.org/10.1105/tpc.107.050427

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title = "Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity",

abstract = "SGT1 (for suppressor of G2 allele of skp1) and RAR1 (for required for Mla12 resistance) are highly conserved eukaryotic proteins that interact with the molecular chaperone HSP90 (for heat shock protein90). In plants, SGT1, RAR1, and HSP90 are essential for disease resistance triggered by a number of resistance (R) proteins. Here, we present structural and functional characterization of plant SGT1 proteins. Random mutagenesis of Arabidopsis thaliana SGT1b revealed that its CS (for CHORD-SGT1) and SGS (for SGT1 specific) domains are essential for disease resistance. NMR-based interaction surface mapping and mutational analyses of the CS domain showed that the CHORD II domain of RAR1 and the N-terminal domain of HSP90 interact with opposite sides of the CS domain. Functional analysis of the CS mutations indicated that the interaction between SGT1 and HSP90 is required for the accumulation of Rx, a potato (Solanum tuberosum) R protein. Biochemical reconstitution experiments suggest that RAR1 may function to enhance the SGT1-HSP90 interaction by promoting ternary complex formation.",

keywords = "DISEASE RESISTANCE PROTEIN, ATPASE ACTIVITY, CO-CHAPERONE, ESSENTIAL COMPONENT, CYTOSOLIC HSP90, CYSTEINE-RICH, RAR1, ARABIDOPSIS, COMPLEX, CONTRIBUTES",

author = "Marta Boter and Beatrice Amigues and Jack Peart and Christian Breuer and Yasuhiro Kadota and Catarina Casais and Geoffrey Moore and Colin Kleanthous and Francoise Ochsenbein and Ken Shirasu and Raphael Guerois",

year = "2007",

month = nov,

doi = "10.1105/tpc.107.050427",

language = "English",

volume = "19",

pages = "3791--3804",

journal = "The Plant Cell",

issn = "1040-4651",

publisher = "American Society of Plant Biologists",

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Boter, M, Amigues, B, Peart, J, Breuer, C, Kadota, Y, Casais, C, Moore, G, Kleanthous, C, Ochsenbein, F, Shirasu, K & Guerois, R 2007, 'Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity', The Plant Cell, vol. 19, no. 11, pp. 3791-3804. https://doi.org/10.1105/tpc.107.050427

TY - JOUR

T1 - Structural and functional analysis of SGT1 reveals that its interaction with HSP90 is required for the accumulation of Rx, an R protein involved in plant immunity

AU - Boter, Marta

AU - Amigues, Beatrice

AU - Peart, Jack

AU - Breuer, Christian

AU - Kadota, Yasuhiro

AU - Casais, Catarina

AU - Moore, Geoffrey

AU - Kleanthous, Colin

AU - Ochsenbein, Francoise

AU - Shirasu, Ken

AU - Guerois, Raphael

PY - 2007/11

Y1 - 2007/11

N2 - SGT1 (for suppressor of G2 allele of skp1) and RAR1 (for required for Mla12 resistance) are highly conserved eukaryotic proteins that interact with the molecular chaperone HSP90 (for heat shock protein90). In plants, SGT1, RAR1, and HSP90 are essential for disease resistance triggered by a number of resistance (R) proteins. Here, we present structural and functional characterization of plant SGT1 proteins. Random mutagenesis of Arabidopsis thaliana SGT1b revealed that its CS (for CHORD-SGT1) and SGS (for SGT1 specific) domains are essential for disease resistance. NMR-based interaction surface mapping and mutational analyses of the CS domain showed that the CHORD II domain of RAR1 and the N-terminal domain of HSP90 interact with opposite sides of the CS domain. Functional analysis of the CS mutations indicated that the interaction between SGT1 and HSP90 is required for the accumulation of Rx, a potato (Solanum tuberosum) R protein. Biochemical reconstitution experiments suggest that RAR1 may function to enhance the SGT1-HSP90 interaction by promoting ternary complex formation.

AB - SGT1 (for suppressor of G2 allele of skp1) and RAR1 (for required for Mla12 resistance) are highly conserved eukaryotic proteins that interact with the molecular chaperone HSP90 (for heat shock protein90). In plants, SGT1, RAR1, and HSP90 are essential for disease resistance triggered by a number of resistance (R) proteins. Here, we present structural and functional characterization of plant SGT1 proteins. Random mutagenesis of Arabidopsis thaliana SGT1b revealed that its CS (for CHORD-SGT1) and SGS (for SGT1 specific) domains are essential for disease resistance. NMR-based interaction surface mapping and mutational analyses of the CS domain showed that the CHORD II domain of RAR1 and the N-terminal domain of HSP90 interact with opposite sides of the CS domain. Functional analysis of the CS mutations indicated that the interaction between SGT1 and HSP90 is required for the accumulation of Rx, a potato (Solanum tuberosum) R protein. Biochemical reconstitution experiments suggest that RAR1 may function to enhance the SGT1-HSP90 interaction by promoting ternary complex formation.

KW - DISEASE RESISTANCE PROTEIN

KW - ATPASE ACTIVITY

KW - CO-CHAPERONE

KW - ESSENTIAL COMPONENT

KW - CYTOSOLIC HSP90

KW - CYSTEINE-RICH

KW - RAR1

KW - ARABIDOPSIS

KW - COMPLEX

KW - CONTRIBUTES

U2 - 10.1105/tpc.107.050427

DO - 10.1105/tpc.107.050427

M3 - Article

C2 - 18032631

SN - 1040-4651

VL - 19

SP - 3791

EP - 3804

JO - The Plant Cell

JF - The Plant Cell

IS - 11

ER -