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Participation of amino acid decarboxylases in biochemical interactions between triticale (Triticosecale; Poaceae) and bird cherry-oat aphid (Rhopalosiphum padi; Aphididae)
Institution:1. Center for Clean Water and Clean Energy, Massachusetts Institute of Technology, Cambridge, MA 02139, United States;2. King Fahd University for Petroleum and Minerals, Dhahran, Saudi Arabia
Abstract:The roles of ornithine decarboxylase, lysine decarboxylase and tyrosine decarboxylase in biochemical interactions of two cultivars of winter triticale (Triticosecale), Tornado and Witon, and bird cherry-oat aphid (Rhopalosiphum padi L.) were determined. Results showed the resistant Witon had higher lysine decarboxylase activity than the susceptible Tornado. There was a significant negative correlation between the density of R. padi populations and lysine decarboxylase activity. Such correlations did not occur for the other decarboxylases. Aphid feeding induced a decrease of lysine decarboxylase activity within both cultivars after one week of infestation and increased its activity after two weeks in the moderately resistant Witon. Ornithine decarboxylase activity was induced in tissues of the susceptible Tornado and inhibited in Witon after two weeks of infestation. Aphid infestations did not change tyrosine decarboxylase activity in Witon, whereas in Tornado it decreased in activity after one day of aphid feeding and then increased after two weeks. It was concluded that of the three enzymes studied, lysine decarboxylase was the most important in the response of winter triticale to infestation by R. padi.
Keywords:Triticale  Amino acid decarboxylases  Plant amines  Polyamines
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