Stimulation of a Ca2+-Calmodulin-activated histone 3 arginine kinase in quiescent rat heart endothelial cells compared to actively dividing cells

Bassam T. Wakim, Patricia S. Grutkoski, Andrew T M Vaughan, Gary L. Engelmann

Research output: Contribution to journalArticle

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Abstract

A Ca2+-calmodulin-activated histone 3 kinase was partially purified from nuclear extracts of dividing and quiescent rat heart endothelial cells. The histone 3 phosphorylating activity was 20-100-fold higher in quiescent than in dividing cells. Base hydrolysis followed by amino acid analysis revealed that histone 3 was phosphorylated on arginine. Further investigations were conducted to determine whether phosphorylation of histone 3 also occurred in vivo. Cells were incubated for 3 h in a phosphate-free medium supplemented with [32P]phosphoric acid. It was observed that the nuclear content of arginine-phosphorylated histone 3 was considerably higher in quiescent than in dividing rat heart endothelial cells. The histone 3 arginine kinase is a component of a complex containing a Ca2+-dependent calmodulin-binding protein of apparent molecular mass of 85 kDa. Using polyclonal antibodies to an 85-kDa protein, also the major Ca2+-dependent calmodulin-binding component of the histone 3 arginine kinase from calf thymus, an immunoreactive protein of identical apparent molecular mass was found to be present in equal amounts both in dividing and quiescent cells. We propose that the 85-kDa protein is either the histone 3 arginine kinase or one of its subunits and that phosphorylation of histone 3 is involved with cell cycle exit in eukaryotes.

Original languageEnglish (US)
Pages (from-to)23155-23158
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number39
StatePublished - Sep 29 1995
Externally publishedYes

Fingerprint

Arginine Kinase
Endothelial cells
Calmodulin
Histones
Rats
Endothelial Cells
Phosphorylation
Molecular mass
Arginine
Protamine Kinase
Calmodulin-Binding Proteins
Proteins
Thymus
Eukaryota
Thymus Gland
Cell Cycle
Hydrolysis
Phosphates
Phosphotransferases
Cells

ASJC Scopus subject areas

  • Biochemistry

Cite this

Stimulation of a Ca2+-Calmodulin-activated histone 3 arginine kinase in quiescent rat heart endothelial cells compared to actively dividing cells. / Wakim, Bassam T.; Grutkoski, Patricia S.; Vaughan, Andrew T M; Engelmann, Gary L.

In: Journal of Biological Chemistry, Vol. 270, No. 39, 29.09.1995, p. 23155-23158.

Research output: Contribution to journalArticle

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