The 90-kDa Heat Shock Protein (hsp90) Induces the Condensation of the Chromatin Structure

P. Csermely, J. Kajtar, M. Hollósi, J. Oikarinen, J. Somogyi

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The 90 kDa heat shock protein (hsp90) is a member of the "chaperone-complex" of steroid receptors believed to be partially or transiently localized in the cell nucleus. Demonstrating that hsp90 has an ATP binding site and autophosphorylating activity we have observed that histones, especially histone H1,are able to modulate the autophosphorylation of hsp90 [Csermely, P. and Kahn, C.R. (1991) J. Biol. Chem. 266, 4943-4950]. Our present data suggest a direct interaction of hsp90 with histones, showing that hsp90 is able to bind histone-agarose and enhances the binding of histones to DNA. Circular dichroism spectra of rat liver chromatin indicate that hsp90 induces a tighter, condensed state of the chromatin structure which is resistant against disruption by high salt treatment. Interactions of hsp90 with the chromatin may be important in regulating the transcriptional activity of steroid receptors and other transcription factors.

Original languageEnglish
Pages (from-to)1657-1663
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume202
Issue number3
DOIs
Publication statusPublished - Aug 15 1994

Fingerprint

HSP90 Heat-Shock Proteins
Heat-Shock Proteins
Histones
Chromatin
Condensation
Steroid Receptors
Circular Dichroism
Cell Nucleus
Liver
Sepharose
Rats
Transcription Factors
Salts
Adenosine Triphosphate
Binding Sites
Cells
DNA

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

The 90-kDa Heat Shock Protein (hsp90) Induces the Condensation of the Chromatin Structure. / Csermely, P.; Kajtar, J.; Hollósi, M.; Oikarinen, J.; Somogyi, J.

In: Biochemical and Biophysical Research Communications, Vol. 202, No. 3, 15.08.1994, p. 1657-1663.

Research output: Contribution to journalArticle

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