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Hsp90-containing multiprotein complexes in the eukaryotic microbe Achlya

S A Brunt1, G H Perdew, D O Toft

  • 1Department of Medical Genetics and Microbiology, University of Toronto, Scarborough Campus, Ontario, Canada.

Cell Stress & Chaperones
|May 19, 1998
PubMed
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Researchers identified heat shock protein 70 (Hsp70) and other proteins in the oomycete Achlya ambisexualis, revealing similarities and unique components in its Hsp90-heterocomplexes compared to vertebrates.

Area of Science:

  • Molecular Biology
  • Mycology
  • Biochemistry

Background:

  • The steroid hormone antheridiol induces sexual differentiation in the oomycete fungus Achlya ambisexualis.
  • Antheridiol binds to a 9S multiprotein complex in A. ambisexualis cytosols, which contains heat shock protein 90 (Hsp90).
  • The full composition of these Achlya Hsp90-heterocomplexes and their homology to vertebrate steroid receptor complexes were previously unknown.

Purpose of the Study:

  • To identify the protein components of the Achlya ambisexualis Hsp90-heterocomplexes.
  • To investigate potential homologies between Achlya Hsp90-heterocomplex components and those found in vertebrate steroid receptor complexes.

Main Methods:

  • Co-immunoprecipitation assays were used to identify proteins that associate with Achlya Hsp90.

Related Experiment Videos

  • Proteins were characterized based on their molecular weight (kDa).
  • Specific protein identifications were confirmed using techniques like relating to known vertebrate proteins and analyzing in vitro translates.

    • Main Results:

    • Multiple cytosolic proteins (110, 74, 64, 61, 56, 47, 27, and 23 kDa) co-immunoprecipitated with Achlya Hsp90.
    • The 74 kDa protein was identified as heat shock protein 70 (Hsp70).
    • The 23 kDa protein showed homology to vertebrate p23, and the 56 kDa protein to immunophilin FKBP51, both known components of vertebrate steroid receptor complexes.
    • Proteins of 110, 61, and 27 kDa appeared unique to Achlya. The 61 kDa protein was specifically found in complexes from antheridiol-treated mycelia.

    Conclusions:

    • Achlya ambisexualis Hsp90-heterocomplexes contain Hsp70, a p23-related protein, and an FKBP51-related protein, sharing some components with vertebrate steroid receptor complexes.
    • The presence of unique proteins, including one induced by antheridiol, suggests distinct regulatory mechanisms in Achlya sexual differentiation.
    • These findings provide insights into the evolution and composition of Hsp90-dependent signaling complexes across different eukaryotic kingdoms.