Soybean β-conglycinin subunit is phosphorylated on two distinct serines by protein kinase CK2 in vitro

Journal of Protein Chemistry

Volumn 18, Issue 3, 1999, Pages 315-323

  Ralet, Marie Christine ^a   Fouques, Dominique ^a   Leonil, Joëlle ^b   Molle, Daniel ^b   Meunier, Jean Claude ^a  

^a AGROPARISTECH   (France)

^b CEMAGREF   (France)

Author keywords

conglycinin; Casein kinase 2; Electrospray; Phosphorylation sites; Protein kinase CK2

Indexed keywords

PROTEIN KINASE; SOYBEAN PROTEIN;

ALPHA CHAIN; ARTICLE; CONSENSUS SEQUENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; SEQUENCE ANALYSIS; SOYBEAN; STRUCTURE ACTIVITY RELATION; YARROWIA LIPOLYTICA;

AMINO ACID SEQUENCE; CASEIN KINASE II; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; FUNGAL PROTEINS; GLOBULINS; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; SERINE; SOYBEAN PROTEINS; SOYBEANS; TIME FACTORS; TRYPSIN;

GLYCINE MAX; YARROWIA LIPOLYTICA;

EID: 53149117440     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1021091413084     Document Type: Article

References (35)

1. Allende, J. E., and Allende, C. C. (1995). Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation, FASEB J. 9, 313-323.
2. Bradford, M. M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
3. Campbell, N. F., Shih, F. F., and Marshall, W. E. (1992). Enzymatic phosphorylation of soy protein isolate for improved functional properties, J. Agric. Food Chem. 40, 403-406.
4. Campbell, N. F., Shih, F. F., Hamada, J. S., and Marshall, W. E. (1996). Effect of limited proteolysis on the enzymatic phosphorylation of soy protein, J. Agric. Food Chem. 44, 759-762.
5. Chan, P.-K., Aldrich, M., Cook, R. G., and Busch, H. (1986). Amino acid sequence of protein B23 phosphorylation site, J. Biol. Chem. 261, 1868-1872.
6. Chardot, T., and Meunier, J.-C. (1994). Purification and principal properties of the casein kinase II purified from the yeast Yarrowia lipolytica, Int. J. Biochem. 26, 1017-1024.
7. Clarke, P. R., and Hardie, D. G. (1990). Regulation of HMG-CoA reductase: Identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver, EMBO J. 9, 2439-2446.
8. Coates, J. B., Medeiros, J. S., Thanh, V. H., and Nielsen, N. C. (1985). Characterization of the subunits of β-conglycinin, Arch. Biochem. Biophys. 243, 184-194.
9. Doyle, J. J., Schuler, M. A., Godette, W. D., Zenger, V., Beachy, R. N., and Slightom, J. L. (1986). The glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris. Structural homologies of genes and proteins, J. Biol. Chem. 261, 9228-9238.
10. Harada, J. J., Barker, S. J., and Goldberg, R. B. (1989). Soybean β-conglycinin genes are clustered in several DNA regions and are regulated by transcriptional and posttranscriptional processes, Plant Cell 1, 415-425.
11. Huddleston, M. J., Annan, R. S., Bean, M. F., and Carr, S. A. (1993). Selective detection of phosphopeptides in complex mixtures by electrospray liquid chromatography/mass spectrometry, J. Am. Soc. Mass Spectrom. 4, 710-717.
12. Kemp, B. E., and Pearson, R. B. (1990). Protein kinase recognition sequence motifs, Trends Biochem. Sci. 15, 342-346.
13. Kennelly, P. J., and Krebs, E. G. (1991). Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases, J. Biol. Chem. 266, 15555-15558.
14. Kinsella, J. E. (1979). Functional properties of soy proteins, J. Am. Oil Chem. Soc. 56, 242-258.
15. Kinsella, J. E., Damodaran, S., and German, B. (1985). Functional properties of oilseed proteins with emphasis on soy, in New Protein Foods (Altschul, A. M., and Wilcke, H. L., eds.), Academic Press, New York, pp. 108-180.
16. Kuenzel, E. A., Mulligan, J. A., Sommercorn, J., and Krebs, E. G. (1987). Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides, J. Biol. Chem. 262, 9136-9140.
17. Mamrack, M. D., Olson, M. O. J., and Busch, H. (1979). Amino acid sequence and sites of phosphorylation in a highly acidic region of nucleolar nonhistone protein C23, Biochemistry 18, 3381-3386.
18. Marchiori, F., Meggio, F., Marin, O., Borin, G., Calderan, A., Ruzza, P., and Pinna, L. A. (1988). Synthetic peptide substrates for casein kinase-2. Assessment of minimum structural requirements for phosphorylation, Biochim. Biophys. Acta 971, 332-338.
19. Marin, O., Meggio, F., Marchiori, F., Borin, G., and Pinna, L. A. (1986). Site specificity of casein kinase-2 (TS) from rat liver cytosol. A study with model peptide substrates, Eur. J. Biochem. 160, 239-244.
20. Meggio, F., Marchiori, F., Borin, G., Chessa, G., and Pinna, L. A. (1984). Synthetic peptides including acidic clusters as substrates and inhibitors of rat liver casein kinase TS (type 2), J. Biol. Chem. 259, 14576-14579.
21. Meggio, F., Marin, O., and Pinna, L. A. (1994). Substrate specificity of protein kinase CK2, Cell. Mol. Biol. Res. 40, 401-409.
22. Mollé, D., and Léonil, J. (1995). Heterogeneity of the bovine κ-casein caseinomacropeptide, resolved by liquid chromatography on-line with electrospray ionization mass spectrometry, J. Chromatogr. A 708, 223-230.
23. Petruccelli, S., and Anon, M. C. (1995). Soy protein isolate components and their interactions, J. Agric. Food Chem. 43, 1762-1767.
24. Pinna, L. A. (1990). Casein kinase 2: An 'eminence grise' in cellular regulation? Biochim. Biophys. Acta 1054, 267-284.
25. Pinna, L. A. (1994). A historical view of protein kinase CK2, Cell. Mol. Biol. Res. 40, 383-390.
26. Ralet, M.-C., Fouques, D., Chardot, T., and Meunier, J.-C. (1996). Enzymatic phosphorylation by a casein kinase II of native and succinylated soy storage proteins glycinin and β-conglycinin, J. Agric. Food Chem. 44, 69-75.
27. Roepstorff, P., and Fohlman, J. (1984). Proposal for a common nomenclature for sequence ions in mass spectra of peptides, Biomed. Mass Spectrom. 11, 601.
28. Ross, L. F. (1989). Optimization of enzymatic phosphorylation of soybean storage proteins: Glycinin and β-conglycinin, J. Agric. Food Chem. 37, 1257-1261.
29. Ross, L. F., and Bhatnagar, D. (1989). Enzymatic phosphorylation of soybean proteins, J. Agric. Food Chem. 37, 841-844.
30. Sebastiani, F. L., Farrell, L. B., Schuler, M. A., and Beachy, R. N. (1990). Complete sequence of a cDNA of α subunit of soybean β-conglycinin, Plant Mol. Biol. 15, 197-201.
31. Seguro, K., and Motoki, M. (1989). Enzymatic phosphorylation of soybean proteins by protein kinase, Agric. Biol. Chem. 53, 3263-3268.
32. Seguro, K., and Motoki, M. (1990). Functional properties of enzymatically phosphorylated soybean proteins, Agric. Biol. Chem. 54, 1271-1274.
33. Shih, F. F., Hamada, J. S., and Marshall, W. E. (1992). Deamidation and phosphorylation to improve protein functionality in foods, in Molecular Approaches to Improving Food Quality and Safety (Bhatnager, D., and Cleveland, T. E., eds.), Van Nostrand Reinhold, New York, pp. 37-59.
34. Small, D., Chou, P. Y., and Fasman, G. D. (1977). Occurrence of phosphorylated residues in predicted β-turns: Implications for β-turn participation in control mechanisms, Biochem. Biophys. Res. Commun. 79, 341-346.
35. Walton, G. M., Spiess, J., and Gill, G. N. (1985). Phosphorylation of high mobility group protein 14 by casein kinase II, J. Biol Chem. 260, 4745-4750.