title: Spermine stimulation of a nuclear NII kinase from pea plumules and its role in the phosphorylation of a nuclear polypeptide.
abstract: We have previously demonstrated that spermine stimulates the phosphorylation of a 47 kilodalton nuclear polypeptide from pea plumules (N Datta, LK Hardison, SJ Roux 1986 Plant Physiol 82: 681-684).  In this paper we report that spermine stimulates the activity of a cyclic AMP independent casein kinase, partially purified from a chromatin fraction of pea plumule nuclei.  This effect of spermine was substrate specific; i.e. with casein as substrate, spermine stimulated the kinase activity, and with phosvitin as substrate, spermine completely inhibited the activity.  The stimulation by spermine of the casein kinase was, in part, due to the lowering of the Mg2+ requirement of the kinase.  Heparin could partially inhibit this casein kinase activity and spermine completely overcame this inhibition.  By further purification of the casein kinase extract on high performance liquid chromatography, we fractionated it into an NI and an NII kinase.  Spermine stimulated the NII kinase by 5- to 6-fold but had no effect on the NI kinase.  Using [gamma-32P]GTP, we have shown that spermine promotes the phosphorylation of the 47 kilodalton polypeptide(s) in isolated nuclei, at least in part by stimulating an NII kinase.
authors.affiliation: Botany Department, University of Texas at Austin 78713, USA.
authors.forename: N
authors.initials: N
authors.lastname: Datta
authors.forename: M B
authors.initials: MB
authors.lastname: Schell
authors.forename: S J
authors.initials: SJ
authors.lastname: Roux
mesh_terms: D047390:Casein Kinase II; D047388:Casein Kinases; D002364:Caseins / Q000378:metabolism; D002467:Cell Nucleus / Q000201:enzymology*; D004268:DNA-Binding Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism / Q000502:physiology; D006493:Heparin / Q000494:pharmacology; D008274:Magnesium / Q000502:physiology; D009687:Nuclear Proteins / Q000378:metabolism* / Q000502:physiology; D018532:Pisum sativum / Q000166:cytology / Q000201:enzymology* / Q000378:metabolism / Q000502:physiology; D010766:Phosphorylation / Q000187:drug effects; D010774:Phosvitin / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism / Q000502:physiology; D018520:Plant Shoots / Q000166:cytology / Q000201:enzymology / Q000378:metabolism / Q000502:physiology; D011494:Protein Kinases / Q000378:metabolism / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism* / Q000502:physiology; D012639:Seeds / Q000166:cytology / Q000201:enzymology* / Q000378:metabolism / Q000502:physiology; D013096:Spermine / Q000494:pharmacology / Q000502:physiology*; D013379:Substrate Specificity
chemical_list: D002364:Caseins; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D010940:Plant Proteins; D013096:Spermine; D006493:Heparin; D010774:Phosvitin; D011494:Protein Kinases; D047390:Casein Kinase II; D047388:Casein Kinases; D017346:Protein Serine-Threonine Kinases; D008274:Magnesium