Journal of Undergraduate Research
Keywords
post-translational modification, cell-free protein synthesis, myristoylation
College
Ira A. Fulton College of Engineering and Technology
Department
Chemical Engineering
Abstract
The purpose of this project was to examine the phenomenon of eukaryotic myristoylation in a prokaryotic cell-free environment. Basically the idea is that eukaryotic cells such as those within humans have a more robust system for synthesizing protein but it is cheaper, faster, and more easily controlled to synthesize protein in bacteria cells. The problem, then, with using bacteria is that it lacks the ability to perform such functions as post-translational modification; in other words, once the protein has been created through RNA transcription separate enzymes add functional groups to the protein. One such modification is myristoylation, which uses the enzyme N-myristoyltransferase (NMT) to attach a fatty acid to the end of the protein. Bacteria such as E. Coli do not naturally have this enzyme present and so are unable to perform myristoylation. Our research has been an attempt to show that myristoylation is possible in a system composed of prokaryotic cell extract with the addition of NMT plasmid.
Recommended Citation
Katz, Anna and Bundy, Dr. Brad
(2013)
"Post-Translational Modification in Cell-Free Protein Synthesis,"
Journal of Undergraduate Research: Vol. 2013:
Iss.
1, Article 1775.
Available at:
https://scholarsarchive.byu.edu/jur/vol2013/iss1/1775