Abstract
Phosphorylation of several synthetic acidic peptides by biochemically isolated casein kinase II (CKII) and by cellular and nuclear extracts containing CKII-like activity has been investigated. Especially the synthetic peptide pyroGlu-Asp-Asp-Ser-Asp-Glu-Glu-Asn comprising the carboxy-terminal acidic hepta-peptide of the largest subunit of RNA polymerase II was found to serve as an excellent substrate for purified CKII. Moreover, this peptide reduces the rate of ‘in vitro’ ATP=dependent stimulation of DNA transcription induced by the proteins in the extracts. Since the peptide itself is also significantly phosphorylated in such assays, it is supposed that it serves as a competitive substrate for the phosphorylation of proteins in the extracts whose phosphorylation seems to be a prerequisite for their activity in the transcription process. This points to the involvement of CKII and substrate(s) of CKII in the process of transcription.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Durban E, Goodenough M, Mills J, Busch H: Topoisomerase I phosphorylation ‘in vitro’ and in rapidly growing Novikoff hepatoma cells. EMBO J 4: 2921–2926, 1985
Stetler DA, Rose KM: Phosphorylation of deoxyribonucleic acid dependent RNA polymerase II by nuclear protein kinase CKII: mechanism of enhanced ribonucleic acid synthesis. Biochemistry 21:3721–3728, 1982
Luscher B, Kuenzel EA, Krebs EG, Eisenman RN: Myc oncoproteins are phosphorylated by casein kinase II. EMBO J 8:1111–1119, 1989
Luscher B, Christenson E, Litchfield DW, Krebs EG, Eisenman RN: Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation. Nature 344:517–521, 1990
Barbosa MS, Edmonds C, Fisher C, Schiller JT, Lowy DR, Vousden KH: The region of the HPV E7 oncoprotein homologous to adenovirus E1a and SV40 large T antigen contains separate domains for Rb binding and casein kinase II phosphorylation. EMBO J 9:153–160, 1990
Pinna LA: Casein kinase II: an ‘eminence grise’ in cellular regulation? Biochim Biophys Acta 105:267–284, 1990
Chillemi F, Lugaro G, Boari D, Durban E: Acidic pentapeptide phosphorylatedin vitro by calf thymus protein kinase NII binds to DNA in the presence of Mg2+ cations. FEBS Lett 291:67–70, 1991
Meek DW, Simon S, Kikkawa U, Echart W: The p53 tumor suppressor protein is phosphorylated at serine 389 by casein kinase II. EMBO J 9:3253–3260, 1990
Coderoni S, Miano A, Barra D, Bramucci M, Felici F, Paparelli M, Amici D, Gianfranceschi GL: Isolation and characterization of small phosphorylated peptides controlling transcription ‘in vitro’ from trout testis chromatin DNA. Physiol Chem Phys Med NMR 20:91–108, 1988
Gianfranceschi GL, Cardellini E, Piccinini G, Bramucci M, Miano A, Maccari E, Amici D, Durban E: Synthetic model peptides phosphorylated ‘in vitro’ by NII kinase and cation-mediated interactions with DNA. Physiol Chem Phys Med NMR 21:289–294 1989
Amici D, Rossi GB, Cioe' L, Matarese GP, Dolei A, Gianfranceschi GL: Low-molecular weight peptide inhibits RNA synthesis in human leukemic and phytohemagglutinin-stimulated leukocytes and globin mRNA transcription in differentiating Friend cells. Proc Natl Acad Sci USA 74:3869–3873, 1977
Gianfranceschi GL, Barra D, Bossa F, Coderoni S, Paparelli M, Venanzi F, Cicconi F, Amici D: Small peptides controlling transcriptionin vitro are bound to chromatin DNA. Biochim Biophys Acta 699:138–148, 1982
Manley JL, Fire A, Cano A, Sharp PA, Gefter ML: DNA-dependent transcription of adenovirus genes in a soluble whole-cell extract. Proc Natl Acad Sci USA 77:3855–3859, 1980
Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685, 1970
Antoni G, Presentini R, Perin F, Tagliabue A, Ghiara P, Censini S, Volpini G, Villa L, Boraschi D: A short synthetic peptide fragment of human interleukin 1 with immunostimulatory but not inflammatory activity. J Immunol 137:3201–3204, 1986
Elgjo K, Reichelt KL: Purification and characterization of a mitosis inhibiting epidermal peptide. Cell Biol Int Rep 5:379–382, 1984
Pleau JM, Dardenne M, Blouquit Y, Bach JF: Amino acid sequence of a circulating thymic factor, a nonapeptide from pig serum. J Biol Chem 252:8045–8050, 1977
Serrano L, Diaz-Nido J, Wandosell F, Avila J: Tubulin phosphorylation by casein kinase II is similar to that foundin vivo. J Cell Biol 105:1732–1739, 1987
Watt FM, Reichelt KL, Elgjo K: Pentapeptide inhibitor of epidermal mitosis: production and responsiveness in cultures of normal, transformed and neoplastic human keratinocytes. Carcinogenesis 10:2249–2253, 1989
Leiva L, Carrasco D, Taylor A, Veliz M, Gonzalez C, Allende C, Allende J: Casein kinase II is a major protein phosphorylating activity in the nuclei of Xenopus laevis oocytes. Biochem Int 14:707–717, 1987
Lin A, Frost J, Deng T, Smeal T, Al-Alawi N, Kikkawa U, Hunter T, Brenner D, Karin M: Casein kinase II is a negative regulator of c-jun DNA binding and AP-1 activity. Cell 70:777–789, 1992
Meggio F, Marchiori F, Borin F, Chessa G, Pinna LA: Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (Type-2). J Biol Chem 259:14576–14579, 1984
Licfield DW, Arendt A, Lozeman FJ, Frebs EG, Hargrave PA, Palczewski K: Synthetic phosphopeptides are substrates for casein kinase II. FEBS Lett 261:117–120, 1990
Cadena DL, Dahmus ME: Messenger RNA synthesis in mammalian cells is catalyzed by the phosphorylated form of RNA polymerase II. J Biol Chem 262:12468–12474, 1987
Payne JM, Laybourn PJ, Dhamus ME: The transition of RNA polymerase II from initiation to elongation is associated with phosphorylation of the carboxyl-terminal domain of subunit IIa. J Biol Chem 26:19621–19629, 1989
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Angiolillo, A., Bramucci, M., Marsili, V. et al. Phosphorylation of synthetic acidic peptides by casein kinase II: evidence for competition with phosphorylation of proteins involved in transcription. Mol Cell Biochem 125, 65–72 (1993). https://doi.org/10.1007/BF00926836
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00926836