Interaction between casein kinase II and the 90-kDa stress protein, HSP90.

Purified casein kinase II (CKII) aggregates and loses activity under physiological salt conditions and within the range of physiological temperatures. In accord with our previous report [Miyata, Y., & Yahara, I. (1992) J. Biol. Chem. 267, 7042-7047], we report here that HSP90 protects CKII from the aggregation and inactivation by forming soluble CKII-HSP90 complexes. Surface plasmon resonance (SPR) measurements revealed that CKII binds to immobilized HSP90 within minutes. The KD of the binding is approximately 10(-7) M. ATP does not influence the interaction. The membrane-overlay method revealed that HSP90 binds to the catalytic CKII alpha subunit. Heparin, which binds to CKII alpha, inhibited the binding of CKII to HSP90-Sepharose. In addition, HSP90 competed with DNA for binding to CKII. Finally, SPR experiments showed that a peptide corresponding to the heparin and DNA binding site of CKII alpha binds to immobilized HSP90. These results indicate that HSP90, DNA, and heparin compete with each other for binding to a common site of CKII alpha. If the binding of CKII to DNA is biologically significant, it could be possibly regulated also by HSP90.