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Screening of Hsp105alpha-binding proteins using yeast and bacterial two-hybrid systems.

Hsp105alpha is a 105-kDa stress protein, which is expressed constitutively at especially high levels in the brain compared with other tissues in mammals, and is also induced by a variety of stressors. Recently, we have shown that Hsp105alpha binds to alpha-tubulin and prevents the heat-induced disaggregation of microtubules. To further elucidate the function of Hsp105alpha, we searched for Hsp105alpha-binding proteins by screening a mouse FM3A cell library and human and mouse brain cDNA libraries using the yeast and bacterial two-hybrid systems. We showed here that Hsp105alpha interacted with several cellular proteins, such as cofilin, dynein light chain 2A, alpha-adducin, ubiquitin activating enzyme E1, phosphoglycerate kinase 1, and platelet-activating factor acethylhydrolase alpha1-subunit. The interaction was validated by the results of a pull-down assay and indirect immunofluorescence analysis. The significance of Hsp105alpha and Hsp105alpha-binding proteins in cells was discussed.

Pubmed ID: 14733918


  • Saito Y
  • Doi K
  • Yamagishi N
  • Ishihara K
  • Hatayama T


Biochemical and biophysical research communications

Publication Data

February 6, 2004

Associated Grants


Mesh Terms

  • Animals
  • Bacterial Proteins
  • Brain
  • COS Cells
  • Calmodulin-Binding Proteins
  • Cytoskeleton
  • DNA, Complementary
  • Fluorescent Antibody Technique, Indirect
  • Fungal Proteins
  • Gene Library
  • HSP110 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • Humans
  • Mice
  • Microscopy, Fluorescence
  • Microtubules
  • Plasmids
  • Protein Binding
  • Protein Biosynthesis
  • Recombinant Proteins
  • Transcription, Genetic
  • Tubulin
  • Two-Hybrid System Techniques