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.
Schnaider
T
T
Department of Medical Chemistry, Semmelweis University, Budapest, Hungary.
Oikarinen
J
J
Ishiwatari-Hayasaka
H
H
Yahara
I
I
Csermely
P
P
D000595:Amino Acid Sequence; D000818:Animals; D004789:Enzyme Activation; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006609:High Mobility Group Proteins / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D020349:Surface Plasmon Resonance
D018841:HSP90 Heat-Shock Proteins; D006609:High Mobility Group Proteins; D006657:Histones; D010446:Peptide Fragments; D010455:Peptides; D011494:Protein Kinases