Interactions of Hsp90 with histones and related peptides

Tamás Schnaider, Jouko Oikarinen, Haruko Ishiwatari-Hayasaka, Ichiro Yahara, Péter Csermely

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27 Citations (Scopus)


The 90 kDa heat shock protein (Hsp90) induces the condensation of the chromatin structure [Csermely, P., Kajtar, J., Hollosi, M., Oikarinen, J., and Somogyi, J. (1994) Biochem. Biophys. Res. Commun. 202, 1657-1663]. In our present studies we used surface plasmon resonance measurements to demonstrate that Hsp90 binds histones H1, H2A, H2B, H3 and H4 with high affinity having dissociation constants in the submicromolar range. Strong binding of the C-terminal peptide of histone H1 containing the SPKK-motif and a pentaeicosa-peptide including the Hsp90 bipartite nuclear localization signal sequence was also observed. However, a lysine/arginine-rich peptide of casein, and the lysine-rich platelet factor 4 did not display a significant interaction with Hsp90. Histones and positively charged peptides modulated the Hsp90-associated kinase activity. Interactions between Hsp90, histones, and high mobility group (HMG) protein-derived peptides raise the possibility of the involvement of Hsp90 in chromatin reorganization during steroid action, mitosis, or after cellular stress.

Original languageEnglish
Pages (from-to)2417-2426
Number of pages10
JournalLife Sciences
Issue number22
Publication statusPublished - Oct 22 1999


  • Chromatin
  • HMG-protein
  • Histone H1
  • Hsp90
  • Nuclear localization
  • Signal

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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  • Cite this

    Schnaider, T., Oikarinen, J., Ishiwatari-Hayasaka, H., Yahara, I., & Csermely, P. (1999). Interactions of Hsp90 with histones and related peptides. Life Sciences, 65(22), 2417-2426.