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. 1978 Sep;62(3):434–437. doi: 10.1104/pp.62.3.434

Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei 1

Michael G Murray 1,2, Thomas J Guilfoyle 1,3, Joe L Key 1
PMCID: PMC1092141  PMID: 16660532

Abstract

A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of 32Pi from γ-[32P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bell G. I., Valenzuela P., Rutter W. J. Phosphorylation of yeast DNA-dependent RNA polymerases in vivo and in vitro. Isolation of enzymes and identification of phosphorylated subunits. J Biol Chem. 1977 May 10;252(9):3082–3091. [PubMed] [Google Scholar]
  2. Chen Y. M., Lin C. Y., Chang H., Guilfoyle T. J., Key J. L. Isolation and Properties of Nuclei from Control and Auxin-treated Soybean Hypocotyl. Plant Physiol. 1975 Jul;56(1):78–82. doi: 10.1104/pp.56.1.78. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dahmus M. E. Stimulation of ascites tumor RNA polymerase II by protein kinase. Biochemistry. 1976 May 4;15(9):1821–1829. doi: 10.1021/bi00654a006. [DOI] [PubMed] [Google Scholar]
  4. Desjardins P. R., Liew C. C., Gornall A. G. Rat liver nuclerar protein kinases. Can J Biochem. 1975 Mar;53(3):354–363. doi: 10.1139/o75-049. [DOI] [PubMed] [Google Scholar]
  5. Gallinaro-Matringe H., Stevenin J., Jacob M. Salt dissociation of nuclear particles containing DNA-like RNA. Distribution of phosphorylated and nonphosphorylated species. Biochemistry. 1975 Jun 3;14(11):2547–2554. doi: 10.1021/bi00682a039. [DOI] [PubMed] [Google Scholar]
  6. Guilfoyle T. J., Lin C. Y., Chen Y. M., Key J. L. Purification and characterization of RNA polymerase I from a higher plant. Biochim Biophys Acta. 1976 Feb 5;418(3):344–357. doi: 10.1016/0005-2787(76)90296-3. [DOI] [PubMed] [Google Scholar]
  7. Guilfoyle T. J. Purification and Characterization of DNA-dependent RNA Polymerases from Cauliflower Nuclei. Plant Physiol. 1976 Oct;58(4):453–458. doi: 10.1104/pp.58.4.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kamiyama M., Dastugue B. Rat liver non-histone proteins: correlation between protein kinase activity and activation of RNA synthesis. Biochem Biophys Res Commun. 1971 Jul 2;44(1):29–36. doi: 10.1016/s0006-291x(71)80154-7. [DOI] [PubMed] [Google Scholar]
  9. Kleinsmith L. J. Phosphorylation of non-histone proteins in the regulation of chromosome structure and function. J Cell Physiol. 1975 Apr;85(2 Pt 2 Suppl 1):459–475. doi: 10.1002/jcp.1040850412. [DOI] [PubMed] [Google Scholar]
  10. Kranias E. G., Schweppe J. S., Jungmann R. A. Phosphorylative and functional modifications of nucleoplasmic RNA polymerase II by homologous adenosine 3':5'-monophosphate-dependent protein kinase from calf thymus and by heterologous phosphatase. J Biol Chem. 1977 Oct 10;252(19):6750–6758. [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Lin P. P. Cyclic nucleotides in higher plants? Adv Cyclic Nucleotide Res. 1974;4(0):439–460. [PubMed] [Google Scholar]
  13. Lin P. P., Key J. L. Lysine-rich histone H1 kinase from soybean hypocotyl. Biochem Biophys Res Commun. 1976 Nov 22;73(2):396–403. doi: 10.1016/0006-291x(76)90721-x. [DOI] [PubMed] [Google Scholar]
  14. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  15. Murray M. G., Guilfoyle T. J., Key J. L. Isolation and Characterization of a Chromatin-associated Protein Kinase from Soybean. Plant Physiol. 1978 Jun;61(6):1023–1030. doi: 10.1104/pp.61.6.1023. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Murray M. G., Key J. L. 2,4-Dichlorophenoxyacetic Acid-enhanced Phosphorylation of Soybean Nuclear Proteins. Plant Physiol. 1978 Feb;61(2):190–198. doi: 10.1104/pp.61.2.190. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rubin C. S., Rosen O. M. Protein phosphorylation. Annu Rev Biochem. 1975;44:831–887. doi: 10.1146/annurev.bi.44.070175.004151. [DOI] [PubMed] [Google Scholar]
  18. Schendel P. F., Wells R. D. The synthesis and purification of (gamma-32P)-adenosine triphosphate with high specific activity. J Biol Chem. 1973 Dec 10;248(23):8319–8321. [PubMed] [Google Scholar]
  19. Takeda M., Matsumura S., Nakaya Y. Nuclear phosphoprotein kinases from rat liver. J Biochem. 1974 Apr;75(4):743–751. doi: 10.1093/oxfordjournals.jbchem.a130447. [DOI] [PubMed] [Google Scholar]

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