Biochemistry & Molecular Biology
Mutagenesis and Purification of Bacterial Carboxylesterase from Francisella tularensis
Document Type
Poster Presentation
Location
Indianapolis, IN
Subject Area
Biochemistry & Molecular Biology
Start Date
11-4-2014 8:30 AM
End Date
11-4-2014 9:30 AM
Sponsor
Jeremy Johnson (Butler University)
Description
Palmitoylation is a lipid modification that is added to proteins and controls the localization of proteins in cells. Cycling of proteins through different palmitoylation states is a central method for controlling protein activity in a cell. Misregulation of palmitoylation is also linked to the development of cancer. I have developed methods for measuring palmitoylation in two different bacteria, the model bacterium E. coli and a metabolically diverse bacterium P. putida. Using a mimic of palmitic acid, all palmitoylated proteins in the two bacteria can be tagged and then visualized by chemical attachment of the palmitoylated proteins to a colored tag. This method is called click chemistry. Click chemistry involves the reaction between an azide and an alkyne that is a biologically inactive reaction. The results of the research will provide tools for studying palmitoylation in bacteria and will identify targets for future antibacterial and cancer treatments.
Mutagenesis and Purification of Bacterial Carboxylesterase from Francisella tularensis
Indianapolis, IN
Palmitoylation is a lipid modification that is added to proteins and controls the localization of proteins in cells. Cycling of proteins through different palmitoylation states is a central method for controlling protein activity in a cell. Misregulation of palmitoylation is also linked to the development of cancer. I have developed methods for measuring palmitoylation in two different bacteria, the model bacterium E. coli and a metabolically diverse bacterium P. putida. Using a mimic of palmitic acid, all palmitoylated proteins in the two bacteria can be tagged and then visualized by chemical attachment of the palmitoylated proteins to a colored tag. This method is called click chemistry. Click chemistry involves the reaction between an azide and an alkyne that is a biologically inactive reaction. The results of the research will provide tools for studying palmitoylation in bacteria and will identify targets for future antibacterial and cancer treatments.