Dual regulation of a chimeric plant serine/threonine kinase by calcium and calcium/calmodulin

Journal of Biological Chemistry

Volumn 271, Issue 14, 1996, Pages 8126-8132

  Takezawa, D ^a   Ramachandiran, S ^a   Paranjape, V ^a   Poovaiah, B W ^a  

^a WASHINGTON STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALMODULIN; PROTEIN SERINE THREONINE KINASE;

ARTICLE; AUTOPHOSPHORYLATION; CALCIUM TRANSPORT; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; ENZYME REGULATION; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; SIGNAL PROCESSING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

NASA DISCIPLINE NUMBER 40-50; NASA DISCIPLINE PLANT BIOLOGY; NASA PROGRAM SPACE BIOLOGY; NON-NASA CENTER;

AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM; CALMODULIN; DNA PRIMERS; MOLECULAR SEQUENCE DATA; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; SPINACIA OLERACEA;

EID: 0029924239     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.14.8126     Document Type: Article

References (48)

1. Poovaiah, B. W., and Reddy, A. S. N. (1993) CRC Crit. Rev. Plant Sci. 12, 185-211
2. Gilroy, S., and Trewavas, A. (1994) Trends Genet. 16, 677-682
3. Clapham, D. E. (1995) Cell 80, 259-268
4. Klee, C. B. (1991) Neurochem. Res. 16, 1059-1065
5. Cohen, P. (1992) Trends Biochem. Sci. 17, 408-413
6. Hunter, T. (1995) Cell 80, 225-236
7. Edelman, A. M., Blumenthal, D. K., and Krebs, E. G. (1987) Annu. Rev. Biochem. 56, 567-613
8. Schulman, H. (1993) Curr. Opin. Cell Biol. 5, 247-253
9. Hanson, P. I., and Schulman, H. (1992) Annu. Rev. Biochem. 61, 559-601
10. Nairn, A. C., and Picciotto, M. R. (1994) Semin. Cancer Biol. 5, 295-303
11. Colbran, R. J., and Soderling, T. R. (1990) Curr. Topics Cell Regul. 31, 181-221
12. Roberts, D. M., and Harmon, A. C. (1992) Annu. Rev. Plant Physiol. Plant Mol. Biol. 43, 375-414
13. Stone, J. M., and Walker J. C. (1995) Plant Physiol. 108, 451-457
14. Veluthambi, K., and Poovaiah, B. W. (1984) Science 223, 167-169
15. Poovaiah, B. W., and Reddy, A. S. N. (1987) CRC Crit. Rev. Plant Sci. 6, 47-103
16. Blowers, D. P., and Trewavas, A. (1987) Biochem. Biophys. Res. Commun. 143, 691-696
17. Watillon, B., Kettman, R., Boxus, P., and Burny, A. (1993) Plant Physiol. 101, 1381-1384
18. Yamagata, K., Goto, K., Kuo, C.-H., Kondo, H., and Miki, N. (1990) Neuron 4, 469-476
19. Kuno, T., Kajimoto, Y., Hashimoto, T., Mukai, H., Shirai, Y., Saheki, S., and Tanaka, C. (1992) Biochem. Biophys. Res. Commun. 184, 1219-1225
20. Patil, S., Takezawa, D., and Poovaiah, B. W. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 4797-4801
21. Laemmli, U. K. (1970) Nature 237, 680-685
22. Takezawa, D., Liu, Z. H., An, G., and Poovaiah, B. W. (1995) Plant Mol. Biol. 27, 693-703
23. Fromm, H., and Chua, N.-H. (1992) Plant Mol. Biol. Rep. 10, 199-206
24. Reddy, A. S. N., Takezawa, D., Fromm, H., and Poovaiah, B. W. (1993) Plant Sci. 94, 109-117
25. Kunkel, T. A., Roberts, J. D., and Zakour, R. A. (1987) Methods Enzymol. 154, 367-382
26. Roskoski, R., Jr. (1983) Methods Enzymol. 99, 3-6
27. Cooper, J. A. (1983) Methods Enzymol. 99, 387-402
28. Hanks, S. K., Quinn, A. M., and Hunter, T. (1988) Science 241, 42-52
29. O'Neil, K. T., and DeGrado, W. F. (1990) Trends Biochem. Sci. 15, 59-64
30. Renner, M., Danielson, M. A., and Falke, J. J. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 6493-6497
31. Schulman, H. (1988) Adv. Second Messenger Phosphoprotein Res. 22, 39-112
32. Kameshita, I., and Fujisawa, H. (1993) J. Biochem. (Tokyo) 113, 583-590
33. Enslen, H., Sun, P., Brickey, D., Soderling, S. H., Klamo, E., and Soderling, T. R. (1994) J. Biol. Chem. 269, 15520-15527
34. Sikela. J. M., and Hahn, W. E. (1987) Proc. Natl. Acad. Sci. U. S. A. 84, 3038-3042
35. Palczewski, K., Subbaraya, I., Gorczca, W. A., Helekar, B. S., Ruiz, C. C., Ohguro, H., Huang, J., Zhao, X., Crabb, J. W., Johnson, R. S., Walsh, K. A., Gray-Keller, M. P., Detwiler, P. B., and Baehr, W. (1994) Neuron 13, 395-404
36. Pongs, O., Lindemeier, J., Zhu, X. R., Theil, T., Engelkamp, D., Krah,-Jentgens, I., Lambecht, H. G., Koch, K. W., Schwemer, J., Rivosecchi, R., Mallart, A., Galceran, J., Canal, I., Barbas, J. A., and Ferrus, A. (1993) Neuron 11, 15-28
37. Ames, J. B., Porumb, T., Tanaka, T., Ikura, M., and Stryer, L. (1995) J. Biol. Chem. 270, 4526-4533
38. Theil, G., Czernik, A. J., Gorelick, F., Nairn, A. C., and Greengard, P. (1988) Proc. Natl. Acad. Sci. U. S. A. 85, 6337-6341
39. Fong, Y.-L., Taylor, W. L., Means, A. R., and Soderling, T. R. (1989) J. Biol, Chem. 264, 16759-16763
40. Leckteig, R., Shenolikar, S., Denner, L., and Kelly, P. T. (1988) J. Biol. Chem. 263, 19232-19239
41. Colbran, R. J. (1993) J. Biol. Chem. 268, 7163-7170
42. James, P., Vorherr, T., and Carafoli, E. (1995) Trends Biochem. Sci. 20, 38-42
43. Tokui, T., Ando, S., and Ikebe, M. (1995) Biochemistry 34, 5173-5179
44. Bush, D. S. (1993) Plant Physiol. 103, 7-13
45. Gilroy, S., Bethke, P. C., and Jones, R. L. (1993) J. Cell Sci. 106, 453-462
46. Jena, P. K., Reddy, A. S. N., and Poovaiah, B. W. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 3644-3648
47. Braam, J., and Davis, R. W. (1990) Cell 60, 357-364
48. Perera, I. Y., and Zielinski, R. E. (1992) Plant Physiol. 100, 812-819