Event Title
Production of Systemin Binding Protein in Response to Wounding of Tomato Plants
Location
CSU
Student's Major
Chemistry and Geology
Student's College
Science, Engineering and Technology
Mentor's Name
Theresa Salerno
Mentor's Department
Chemistry and Geology
Mentor's College
Social and Behavioral Sciences
Description
Systemin, the first peptide hormone to be isolated in plants, has been shown to be a primary signal of protease inhibitor induction by wounding. A 50-kDa systemin binding protein (SBP-50) has been shown to bind systemin in vitro; however, the precise function, mechanism and regulation of the binding protein remain unknown. To determine, in part, the role of SBP-50 in the wound response, relative SBP-50 concentrations were measured in wounded versus non-wounded tomato leaves. A polymer-two phase system of Dextran T500 and PEG 3350 was used to isolate the components of the tomato leaf plasma membranes. A biotinylated systemin derivative was incubated with the plasma membrane fraction to specifically bind SBP-50, and the two proteins were crosslinked. The membrane components were then separated by gel electrophoresis, and Western blotting was employed to detect the biotin label, and therefore any protein bound to systemin.
Production of Systemin Binding Protein in Response to Wounding of Tomato Plants
CSU
Systemin, the first peptide hormone to be isolated in plants, has been shown to be a primary signal of protease inhibitor induction by wounding. A 50-kDa systemin binding protein (SBP-50) has been shown to bind systemin in vitro; however, the precise function, mechanism and regulation of the binding protein remain unknown. To determine, in part, the role of SBP-50 in the wound response, relative SBP-50 concentrations were measured in wounded versus non-wounded tomato leaves. A polymer-two phase system of Dextran T500 and PEG 3350 was used to isolate the components of the tomato leaf plasma membranes. A biotinylated systemin derivative was incubated with the plasma membrane fraction to specifically bind SBP-50, and the two proteins were crosslinked. The membrane components were then separated by gel electrophoresis, and Western blotting was employed to detect the biotin label, and therefore any protein bound to systemin.
