Modulation of nuclear matrix protein phosphorylation by histones: Possible involvement of NM-associated protein kinase CK2 activity

Sherif Tawfic, Alan T. Davis, Russell A. Faust, Markus Gapany, Khalil Ahmed

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Nuclear matrix (NM), a proteinaceous network of filaments, dictates nuclear morphology and the structure/function of DNA. Phosphorylation of NM proteins is a potential signal for regulating matrix functions. Histones also are intimately involved in DNA structure and transcription. Here, we report that various histones enhanced 32P incorporation into certain NM proteins. Modulation of NM protein phosphorylation by histones is mediated through regulation of protein kinase CK2, a messenger-independent serine/threonine kinase, which is significantly associated with the NM. The stimulatory effect of histones was mitigated by prior incubation of histones with DNA in the reaction. Phosphorylation of NM proteins was extensively reduced when an excess of the CK2-specific peptide substrate was included in the phosphorylation reaction as a competitor. Also, enhancement in the NM- associated CK2 activity by histories was blocked by inhibitors of CK2. Histone H1 effect appeared to be mediated mainly by charge effect since a stretch of polylysine induced a similar effect. Various histones also differentially affected the autophosphorylation of NM-associated CK2 subunits. This may contribute to the observed effects of histones on the NM, resulting in an enhancement and differential pattern of NM protein phosphorylation. Such a regional modification of NM protein phosphorylation might influence the nuclear functions that require histone displacement, namely, replication and transcription.

Original languageEnglish (US)
Pages (from-to)242-250
Number of pages9
JournalJournal of Cellular Biochemistry
Volume72
Issue number2
DOIs
StatePublished - Jan 15 1999

Keywords

  • DNA
  • Histones
  • Nuclear matrix
  • Protein kinase CK2
  • Protein phosphorylation

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