Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants

J Biol Chem. 2004 Jan 16;279(3):2101-8. doi: 10.1074/jbc.M310029200. Epub 2003 Oct 28.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / physiology*
  • Immunity, Innate
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics*
  • Plant Proteins / chemistry
  • Plant Proteins / genetics*
  • Plant Proteins / physiology*
  • Protein Conformation
  • Tobacco / immunology*
  • Tobacco / virology
  • Tobacco Mosaic Virus

Substances

  • HSP90 Heat-Shock Proteins
  • Nuclear Proteins
  • Plant Proteins
  • R protein, Zea mays

Associated data

  • GENBANK/AY368904
  • GENBANK/AY368905
  • GENBANK/AY368906
  • GENBANK/AY368907