Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants.
SGT1 and Rar1 are important signaling components of resistance (R) gene-mediated plant innate immune responses. Here we report that SGT1 and Rar1 associate with the molecular chaperone Hsp90. In addition, we show that Hsp90 associates with the resistance protein N that confers resistance to tobacco mosaic virus. This suggests that Hsp90-SGT1-Rar1 and R proteins might exist in one complex. Suppression of Hsp90 in Nicotiana benthamiana plants shows that it plays an important role in plant growth and development. In addition, Hsp90 suppression in NN plants compromises N-mediated resistance to tobacco mosaic virus. Our results reveal a new role for SGT1- and Rar1-associated chaperone machinery in R gene-mediated defense signaling.
Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.
Yule
Y
Liu
Tessa
T
Burch-Smith
Michael
M
Schiff
Suhua
S
Feng
Savithramma P
SP
Dinesh-Kumar
D000595:Amino Acid Sequence; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology*; D007113:Immunity, Innate; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics*; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D011487:Protein Conformation; D014026:Nicotiana / Q000276:immunology* / Q000821:virology; D014027:Tobacco Mosaic Virus
D018841:HSP90 Heat-Shock Proteins; D009687:Nuclear Proteins; D010940:Plant Proteins; C085200:R protein, Zea mays