Role of protein kinase CK2 in phosphorylation nucleosomal proteins in relation to transcriptional activity.
Protein kinase CK2 undergoes rapid translocation to nuclear matrix and nucleosomes on androgenic stimulation of growth in prostatic epithelial cells. Further, CK2 appears to be regulated differentially in the transcriptionally active and inactive nucleosomes. We have investigated the role of CK2 in phosphorylation of nucleosome-associated proteins in the transcriptionally active and inactive nucleosomes that were isolated from ventral prostate subjected to different androgenic status in vivo. Proteins associated with these nucleosomes were phosphorylated via the intrinsic protein kinase activity, using [gamma-32P]ATP in the absence and presence of GTP. Several proteins appear to be potential substrates for CK2 associated with the nucleosomes. Among them are proteins that are differentially associated with the transcriptionally active and inactive nucleosomes. Phosphorylation of several of these proteins is modulated depending not only on their sites of association (i.e., active vs. inactive nucleosomes) but also on the state of transcriptional activity. Differential phosphorylation of specific proteins by CK2 associated with the active and inactive nucleosomes may be pertinent to the process of transcription regulation.
Guo
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C
Department of Laboratory Medicine and Pathology, University of Minnesota and the Department of Veterans Affairs Medical Center, Minneapolis 55417, USA.
Davis
A T
AT
Yu
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S
Tawfic
S
S
Ahmed
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K
D000818:Animals; D047390:Casein Kinase II; D008297:Male; D009707:Nucleosomes / Q000378:metabolism*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D014158:Transcription, Genetic
D009707:Nucleosomes; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases