Role of protein kinase CK2 in phosphorylation of nucleosomal proteins in relation to transcriptional activity

Chuanhai Guo, Alan T. Davis, Shihui Yu, Sherif Tawfic, Khalil Ahmed

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

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 [γ-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.

Original languageEnglish (US)
Pages (from-to)135-142
Number of pages8
JournalMolecular and cellular biochemistry
Volume191
Issue number1-2
DOIs
StatePublished - 1999

Keywords

  • Androgen action
  • CK2
  • Non-histone proteins
  • Nuclear matrix
  • Nucleosome
  • Prostate
  • Transcription

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