Physical Dissection of the Structural Elements Responsible for Regulatory Properties and Intersubunit Interactions of Protein Kinase CK2 
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- 作者：Oriano Marin ; Flavio Meggio ; Stefania Sarno ; and Lorenzo A. Pinna
- 刊名：Biochemistry
- 出版年：1997
- 出版时间：June 10, 1997
- 年：1997
- 卷：36
- 期：23
- 页码：7192 - 7198
- 全文大小：204K
- 年卷期：v.36,no.23(June 10, 1997)
- ISSN：1520-4995
文摘
The noncatalytic 
-subunit of protein kinase CK2 hasbeen shown to display various and insome respects antagonistic effects on the catalytic 
-subunit[Boldyreff et al. (1993) Biochemistry 32,12672-12677; Meggio et al. (1994) Biochemistry 33,4336-4342]. We have now examined the abilityof peptides encompassing the N- and C-terminal regions of the-subunit ([1-77] and [155-215])tomimic the functions of the whole-length -subunit. Peptide[155-215] possesses only the positive featuresof the -subunit in that it prevents thermal inactivation andstimulates basal activity of the -subunit,while it does not inhibit but rather stimulates calmodulinphosphorylation. In sharp contrast, peptide[1-77] neither protects the -subunit nor stimulates itsbasal activity, while acting as a powerful andspecific inhibitor of calmodulin phosphorylation. Peptide[155-215], but not peptide [1-77],stablyinteracts with -subunit and also displays remarkableself-associating properties. A shorter derivative of[155-215], [170-215], displaying weakerstimulatory properties fails to stably interact with the-subunit and to give rise to dimeric/multimeric forms. Thesedata show that the elements responsiblefor the negative regulation are concentrated in the N-terminal moietyof the -subunit, whereas theC-terminal region retains the beneficial properties of the -subunitand is capable of self-association andbinding of the -subunit. Residues between 155 and 170 arenecessary for the latter functions.
-subunit of protein kinase CK2 hasbeen shown to display various and insome respects antagonistic effects on the catalytic -subunit[Boldyreff et al. (1993) Biochemistry 32,12672-12677; Meggio et al. (1994) Biochemistry 33,4336-4342]. We have now examined the abilityof peptides encompassing the N- and C-terminal regions of the-subunit ([1-77] and [155-215])tomimic the functions of the whole-length -subunit. Peptide[155-215] possesses only the positive featuresof the -subunit in that it prevents thermal inactivation andstimulates basal activity of the -subunit,while it does not inhibit but rather stimulates calmodulinphosphorylation. In sharp contrast, peptide[1-77] neither protects the -subunit nor stimulates itsbasal activity, while acting as a powerful andspecific inhibitor of calmodulin phosphorylation. Peptide[155-215], but not peptide [1-77],stablyinteracts with -subunit and also displays remarkableself-associating properties. A shorter derivative of[155-215], [170-215], displaying weakerstimulatory properties fails to stably interact with the-subunit and to give rise to dimeric/multimeric forms. Thesedata show that the elements responsiblefor the negative regulation are concentrated in the N-terminal moietyof the -subunit, whereas theC-terminal region retains the beneficial properties of the -subunitand is capable of self-association andbinding of the -subunit. Residues between 155 and 170 arenecessary for the latter functions.