Manipulating of 14-3-3 protein expression resultes in the changes of catecholamine content in potato plant

• Autorzy: Wilczynski G. , Kulma A. , Feiga I. , Wenczel A. , Szopa J.
• Języki publikacji: EN

Abstrakty

EN

Recently transgenic potato plants were created where the 14-3-3 protein derived from Cucurbita pepo was overexpressed or potato endogenous 14-3-3 protein repressed. Detailed analysis of those plants suggested that a isolated 14-3-3 isoforms are involved in the control of plant senescence and carbohydrate metabolism. In this study carbohydrate content, adenine nucleotide level and catecholamine content in tubers and leaves of transgenic plants grown in greenhouse and in a field were compared. Overexpressing of 14-3-3 protein gave rise to increase catecholamine contents and soluble sugars in leaves and a reduction in tubers size and starch content. The repression of 14-3-3 synthesis led to opposite effect, a decrease in catecholamine, soluble sugars contents in leaves, and an increase in tubers size and starch content. It is proposed that 14-3-3 protein affects carbohydrate metabolism in potato via regulation of catecholamine synthesis.

Słowa kluczowe

EN

Solanum tuberosum; starch content; transgenic plant; leaf; carbohydrate; protein expression; tuber; metabolism; catecholamine; sugar content; adenine nucleotide; plant senescence; protein; potato; protein content; Cucurbita pepo; transgenic potato; plant

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 1998
• Tom: 03
• Numer: 1
• Opis fizyczny: p.75-91,fig.

Twórcy

autor

Wilczynski G.

• University of Wroclaw, Przybyszewskiego 63-77, 51-148 Wroclaw, Poland

autor

Kulma A.

autor

Feiga I.

autor

Wenczel A.

autor

Szopa J.

Bibliografia

• 1. Aitken A., Collinge D. B., van Heuseden B. P. H., Isobe T., Roseboom P. H. and Rosenfeld G., Soll J. TIBS 17 (1992) 498-501
• 2. Wilczyński G., Kulma A., Markiewicz E. and Szopa J. Cell. Mol. Biol. Lett. 2 (1997) 239-241
• 3. Aitken A. TIBS 20 (1995) 95-97
• 4. Burbelo P. D. and Hall A. Curr. Biol. 5 (1995) 95-96
• 5. Reuther G. W., Fu H., Cripe L. D., Collier R. J. and Rendergast A. M. (1994) Science 266, 129-133
• 6. Fu H., Xia K. and Pallas D. C., Science 266, (1994) 126-129
• 7. Morrison D. Science 266 (1994) 56-57
• 8. Conklin D. S., Galaktionov K. and Beach D. Proc. Natl. Acad. Sci. USA 92 (1995) 7892-7896
• 9. Moorhead G., Douglas P., Monice N., Scarabel M., Aitken A. and MacKintosh C. Curr. Biol. 9 (1996) 1104-1113
• 10. Szopa J. J. Plant Physiol. 144 (1994) 617-619
• 11. Szopa J. Acta Biochim. Polon. 42 (1995) 183-190
• 12. Markiewicz E., Wilczyński G., Rzepecki R., Kulma A. and Szopa J. Cell. Mol. Biol Lett. 1 (1996) 391-415
• 13. Murashige T. and Skoog F. Physiol. Plant. 51 (1962) 493-497
• 14. Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual, 2nd ed. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), 1989
• 15. Deblaere R., Bytebier B., de Greve H., Deboeck F., Schell J., Van Montagu M. and Leemans J. Nucl. Acids Res. 13 (1985) 4777-4788
• 16. Vervliet G., Holsters M., Teuchy H., Van Montagu M. and Schell J. J. Gen. Virol. 26, (1975) 33-48
• 17. Wilczyński G., Kulma A., Sikorski A. F. and Szopa J. J. Plant Physiol 151 (1997) 689-698
• 18. Rocha-Sosa M., Sonnewald U., Frommer W., Stratmann M., Schell J. and Willmitzer L. EMBO J. 8 (1989) 23-29
• 19. Szopa J. and Rose K. M. J. Biol. Chem. 261 (1986) 9022-9028
• 20. Neuhaus H. E. and Stitt M. Planta 182 (1990) 445-454
• 21. Steiner A. L. Methods in Enzymology 38 (1974) 96-105
• 22. Stitt M. R., Lilley R. Mc. C., Gerhardt R. and Heldt H. W. Methods in Enzymology 174 (1989) 518-552
• 23. Szopa J. and Müller-Röber B. Plant Cell Rep. 14 (1994) 180-183
• 24. Takimoto A., Kaihara S., Shinozaki M. and Miura J. Plant Cell Physiol. 32 (1991) 283-289