Surface plasmon resonance analysis shows that the carboxy-terminal domain of Grp94 (Grp94-CT, residues 518-803) physically interacts with the catalytic subunit of protein kinase CK2 (CK2α) under non-stressed conditions. A KD of 4×10-7 was determined for this binding. Heparin competed with Grp94-CT for binding to CK2α. CK2β also inhibited the binding of Grp94-CT to CK2α, and CK2 holoenzyme reconstituted in vitro was unable to bind Grp94-CT. The use of CK2α mutants made it possible to map the Grp94-CT binding site to the four lysine stretch (residues 74-77) present in helix C of CK2α. Grp94-CT stimulated the activity of CK2α wild-type but was ineffective on the CK2α K74-77A mutant. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
|Publication status||Published - 7 Sep 2001|
- Molecular chaperone
- Protein kinase CK2
- Surface plasmon resonance