Mechanism of dimer formation of the 90-kDa heat-shock protein.

@article{Nemoto1995MechanismOD,
  title={Mechanism of dimer formation of the 90-kDa heat-shock protein.},
  author={Tadashi Nemoto and Yuko Ohara-Nemoto and Motonori Ota and Tetsuo Takagi and Kenji Yokoyama},
  journal={European journal of biochemistry},
  year={1995},
  volume={233 1},
  pages={1-8}
}
This study describes the mechanism of homodimer formation of the 90-kDa heat-shock protein (HSP90). In eukaryotic cells, there are two HSP90 isoforms, alpha and beta, encoded by two separate genes. HSP90 alpha exists predominantly as a homodimer, HSP90 beta mainly as a monomer. Analysis by native PAGE revealed that bacterially expressed HSP90 alpha fused to glutathione S-transferase (GST) existed as a high-molecular-mass oligomer, and was converted to a homodimer following removal of the fusion… CONTINUE READING
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