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.

This document is currently not available here.

Share

COinS
 

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.