Interactions of Hsp90 with histones and related peptides.

The 90 kDa heat shock protein (Hsp90) induces the condensation of the chromatin structure [Csermely, P., Kajtár, J., Hollósi, 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.

[1]  P. Csermely,et al.  Signalling and transport through the nuclear membrane. , 1995, Biochimica et biophysica acta.

[2]  E. Baulieu,et al.  Nuclear localization of two steroid receptor-associated proteins, hsp90 and p59. , 1990, Experimental cell research.

[3]  E. Baulieu,et al.  Mutational analysis of Hsp90 alpha dimerization and subcellular localization: dimer disruption does not impede "in vivo' interaction with estrogen receptor. , 1996, Journal of cell science.

[4]  M. Bustin,et al.  Immunochemical analysis of the exposure of high mobility group protein 14 and 17 surfaces in chromatin. , 1990, The Journal of biological chemistry.

[5]  T. Hara,et al.  Reversal of heparin inhibition of nuclear protein kinase NII by polyamines and histones , 1981, FEBS letters.

[6]  W. Welch,et al.  Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases. , 1999, Cell stress & chaperones.

[7]  J. Reinstein,et al.  Assessment of the ATP Binding Properties of Hsp90 (*) , 1996, The Journal of Biological Chemistry.

[8]  G. Hathaway,et al.  Inhibition of casein kinase II by heparin. , 1980, The Journal of biological chemistry.

[9]  C. Kahn,et al.  The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity. , 1991, The Journal of biological chemistry.

[10]  D. DeFranco,et al.  Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. , 1999, Molecular endocrinology.

[11]  P. Csermely,et al.  The 90 kDa heat shock protein (hsp90) induces the condensation of the chromatin structure. , 1994, Biochemical and biophysical research communications.

[12]  G. Hathaway,et al.  Casein kinases--multipotential protein kinases. , 1982, Current topics in cellular regulation.

[13]  T. Grundström,et al.  Nucleotide and calcium‐induced conformational changes in histone H1 , 1997, FEBS letters.

[14]  F. Young.  Biochemistry , 1955, The Indian Medical Gazette.

[15]  W. Pratt,et al.  Steroid receptor interactions with heat shock protein and immunophilin chaperones. , 1997, Endocrine reviews.

[16]  A. Wolffe,et al.  Incorporation of chromosomal proteins HMG‐14/HMG‐17 into nascent nucleosomes induces an extended chromatin conformation and enhances the utilization of active transcription complexes. , 1995, The EMBO journal.

[17]  P. Csermely,et al.  Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study. , 1997, Life sciences.

[18]  Bernd Bukau,et al.  The Hsp70 and Hsp60 Chaperone Machines , 1998, Cell.

[19]  M J Schlesinger,et al.  The dynamic state of heat shock proteins in chicken embryo fibroblasts , 1986, The Journal of cell biology.

[20]  C. Hill,et al.  Histone‐DNA interactions and their modulation by phosphorylation of ‐Ser‐Pro‐X‐Lys/Arg‐ motifs. , 1991, The EMBO journal.

[21]  L. Pinna,et al.  Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase-2 and casein kinase-1. , 1990, European journal of biochemistry.

[22]  M. Miyagi,et al.  Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins , 1992, The Journal of cell biology.

[23]  L. Pearl,et al.  Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone , 1997, Cell.

[24]  F. Hartl.  Molecular chaperones in cellular protein folding , 1996, Nature.

[25]  J. Buchner,et al.  Hsp90 & Co. - a holding for folding. , 1999, Trends in biochemical sciences.

[26]  M. Parker,et al.  Comparison of the 90-kilodalton heat shock protein interaction with in vitro translated glucocorticoid and estrogen receptors. , 1992, Molecular endocrinology.

[27]  Y. Miyata,et al.  Interaction between casein kinase II and the 90-kDa stress protein, HSP90. , 1995, Biochemistry.

[28]  P. Chambon,et al.  Several regions of human estrogen receptor are involved in the formation of receptor-heat shock protein 90 complexes. , 1990, The Journal of biological chemistry.

[29]  M. Bustin,et al.  Modular structure of chromosomal proteins HMG-14 and HMG-17: definition of a transcriptional enhancement domain distinct from the nucleosomal binding domain , 1995, Molecular and cellular biology.

[30]  T. Grundström,et al.  DNA binding of histone H1 is modulated by nucleotides , 1992, FEBS letters.

[31]  G. Goodwin,et al.  Chromosomal proteins. The amino terminal sequence of high mobility group non-histone chromosomal protein HMG 14, showing sequence homologies with two other chromosomal proteins. , 2009, International journal of peptide and protein research.

[32]  A. Csordás,et al.  On the biological role of histone acetylation. , 1990, The Biochemical journal.