Abstract
The gene-inducing property of CK2α, a Ser/Thr protein kinase that appears normally to be complexed to a CK2β protein controlling activity and substrate selectivity, has been unclear. We show here that CK2α induces in human JEG-3 cells the expression of Aromatase, an estrogen-synthesis key enzyme, which is regulated at transcriptional level. Electrophoretic mobility shift assays indicate that CK2α binds to the Aromatase gene promoter. To test for CK2α's transactivating ability as a DNA-binding protein, a CK2α binding site was cloned in front of indicator genes. The constructs were used to transform a yeast-based one-hybrid system. Overexpression of activation-domain fused CK2α in this system, i.e., CK2α in its native configuration, failed to activate the transcription machinery. The data indicate CK2α to affect gene expression at the level of transcription via an indirect as yet unknown mechanism rather than directly as a DNA-binding transcription-activating protein.
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Ackermann, K., Pyerin, W. Protein kinase CK2a may induce gene expression but unlikely acts directly as a DNA-binding transcription-activating factor. Mol Cell Biochem 191, 129–134 (1999). https://doi.org/10.1023/A:1006813004474
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DOI: https://doi.org/10.1023/A:1006813004474