Changes in activity of triticale tyrosine decarboxylase caused by grain aphid feeding

• Autorzy: Sempruch C. , Leszczynski B. , Wojcicka A. , Makosz M. , Chrzanowski G. , Matok H.
• Języki publikacji: EN

Abstrakty

EN

The aim of our study was to quantify changes in the activity of tyrosine decarboxylase (TYDC) within tissues of two cultivars of winter triticale: Triticosecale (Wittm. ex A. Camus), caused by grain aphid, and Sitobion avenae (F.). Obtained results show that Witon cv was less acceptable by S. avenae than Tornado cv and that antibiosis was an important part of the acceptability. The grain aphid feeding on aerial parts of more acceptable Tornado cv caused fluctuations in TYDC activity instead of on less acceptable Witon cv, and a constant increase in enzyme activity was observed. Changes in the TYDC activity within the triticale tissues had a systemic character, since they were present not only in aerial parts directly attacked by the pest, but also within root tissues. It suggests that induction of the enzyme activity is related to an antibiotic response of the triticale towards the grain aphid.

• Wydawca: -
• Czasopismo: Polish Journal of Environmental Studies
• Rocznik: 2009
• Tom: 18
• Numer: 5
• Opis fizyczny: p.901-906,fig.,ref.

Twórcy

autor

Sempruch C.

• Department of Biochemistry and Molecular Biology, University of Podlasie, Prusa 12, 08-110 Siedlce, Poland

autor

Leszczynski B.

• Department of Biochemistry and Molecular Biology, University of Podlasie, Prusa 12, 08-110 Siedlce, Poland

autor

Wojcicka A.

• Department of Biochemistry and Molecular Biology, University of Podlasie, Prusa 12, 08-110 Siedlce, Poland

autor

Makosz M.

• Department of Biochemistry and Molecular Biology, University of Podlasie, Prusa 12, 08-110 Siedlce, Poland

autor

Chrzanowski G.

• Department of Biochemistry and Molecular Biology, University of Podlasie, Prusa 12, 08-110 Siedlce, Poland

autor

Matok H.

• Department of Biochemistry and Molecular Biology, University of Podlasie, Prusa 12, 08-110 Siedlce, Poland

Bibliografia

• 1. FACCHINI, P.J., HUBNER-ALLANACH K.L., TARI L.W. Plant aromatic L-amino acid decarboxylases: evolution, biochemistry, regulation and metabolic engineering applications. Phytochemistry 54, 121, 2000.
• 2. KULMA A., SZOPA J. Catecholoamines are active compounds in plants. Plant Sci. 172, 433, 2007.
• 3. HAGEL J.M., FACCHINI P.J. Elevated tyrosine decarboxylase and tyramine hydroxycinnamoyltransferase levels increase wound-induced tyramine-derived hydroxycinnamic acid amide accumulation in transgenic tobacco leaves. Planta 221, 904, 2005.
• 4. GUILLET G., DE LUCA V. Wound inducible biosynthesis of phytoalexin hydroxycinnamic acid amides of tyramine in tryptophan and tyrosine decarboxylase transgenic tobacco lines. Plant Physiol. 137, 692, 2006.
• 5. GOGGIN F.L. Plant-aphid interactions: molecular and ecological perspectives. Cur. Opinion Plant Biol. 10, 399, 2007.
• 6. GROPPA M.D., BENAVIDES M.P. Polyamines and abiotic stress: recent advances. Amino Acids 34, 35, 2008.
• 7. CHEN H., JONES D.A., HOWE G.A. Constitutive activation of the jasmonate signaling pathways enhances the production of secondary metabolites in tomato. FEBS Lett. 580, 2540, 2006.
• 8. FACCHINI P.J. Temporal correlation of tyramine metabolism with alkaloid and amide biosynthesis in elicited opium poppy cell cultures. Phytochemistry 49, 481, 1998.
• 9. KRISTIANSEN B.K., BURHENNE K., RASMUSSEN S.K. Peroxidases and the metabolism of hydroxycinnamic acid amide in Poaceae. Phytochem. Rev. 3, 127, 2004.
• 10. LEE D.E., KANG K., LEE S.G., BACK K. Enhanced synthesis of feruloyltyramine and 4-coumaroyltyramine in associated with tyramine availability in transgenic rice expressing pepper tyramine N-hydroxycinnamoyltransferase. Plant Sci. 172, 57, 2007.
• 11. PETERSON D.M., DIMBERG L.H. Avenanthramide concentration and hydroxycinnamoyl-CoA : hydroxyanthranilate N-hydroxycinnamoyltransferase activities in developing oats. J. Cereal Sci. 47, 101, 2008.
• 12. FIXON-OWOO S., LAVASSEUR F., WILLIAMS K., SABADO T.N., LOWE M., KLOSE M., MERCIER A.J., FIELDS P., ATKINSON J. Preparation and biological assessment of hydroxycinnamic acid amides of polyamines. Phytochemistry 63, 315, 2003.
• 13. STRØMGAARD K., JENSEN L.S., VOGENSEN S.B. Polyamine toxins: development of selective ligands for ionotropic receptors. Toxicon 45, 249, 2005.
• 14. KLOSE M.K., ATKINSON J.K., MERCIER A.J. Effect of hydroxy-cinnamoyl conjugate of spermidine on arthropod neuromuscular junctions. J. Comp. Physiol. 187, 945, 2002.
• 15. SEMPRUCH C. Activity of tyrosine decarboxylase in winter triticale attacked by grain aphid (Sitobion avenae F.). Pestycydy/Pesticides 4, 149, 2005.
• 16. WRATTEN S.D., LEE G., STEVENS D.J. Duration of cereal aphids population and the effects on yield and quality. Proceedings of 1979 British Crop Protection Conference -Pest and Diseases, 1, 1979.
• 17. LYKOURESSIS D. A comparative study of different aphid population parameters in assessing resistance in cereals. Z. Angew. Entomol. 97, 77, 1984.
• 18. TOTTMAN D.R., BROAD H. T he decimal code for the growth stages of cereals, with illustrations. Ann. Appl. Biol. 93, 221, 1987.
• 19. WYATT I.J., WHITE P.F. Simple estimation of intrinsic rates for aphids and tetranychid mite. J. Appl. Ecol. 14, 757, 1977.
• 20. TJALLINGII W.F. Aphids, Their Biology, Natural Enemies and Control, Vol. B; Elsevier: Amsterdam, pp 95-108, 1988.
• 21. PHAN A.P.H., NGO T.T., LENHOFF H.M. Tyrosine decarboxylase. Spectrophotometric assay and application determining pyridoxal-5’-phosphate. Appl. Biochem. Biotech. 8, 127, 1983.
• 22. LOWRY J.O.H., ROSEBROUGH N.J., FARR A.L., RANDAL R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 256, 1951.
• 23. CIEPIELA A.P., SEMPRUCH C., SPRAWKA I., CHRZANOWSKI G. Evaluation of antibiotic properties and tolerance of winter triticale cultivars to grain aphid in Central-Eastern Poland. Aphids and Other Hemipterous Insects 7, 187, 1999.
• 24. CAILLAUD C.M., DEDRYVER C.A., DI PIETRO J.P., SIMON J.C., FIMA F., CHAUBET B. Clonal variability in the response of Sitobion avenae (Homoptera: Aphididae) to resistant and susceptible wheat. Bull. Entomol. Res. 85, 189, 1995.
• 25. LESZCZYŃSKI B. Allelopathy Update, vol. II, Basic and Applied Aspects; Science Publishers Inc.: Enfield, pp 285-320, 1999.
• 26. GOŁAWSKA S., LESZCZYŃSKI B., OLESZEK W. Effect of low and high-saponin lines of alfalfa on pea aphid. J. Insect Physiol. 52, 737, 2006.
• 27. SEMPRUCH C., CIEPIELA A.P. Free amino acids of winter triticale ears settled by grain aphid. Aphids and Other Homopterous Insects 6, 55, 1998.
• 28. CIEPIELA A.P., SEMPRUCH C., CHRZANOWSKI G. Evaluation of natural resistance of winter triticale cultivars against a grain aphid using food coefficients. Jour. Appl. Entomol. 123, 491, 1999.
• 29. ABBOT K.C., MORRIS W.F., GROSS K. Simultaneous effects of food limitation and inducible resistance on herbivore population dynamics. Theoret. Popul. Biol. 73, 63, 2008.