ISOLATION OF A 55 kD PROTEIN THAT SPECIFICALLY BINDS THE 3′ AU-RICH ELEMENT OF INTERLEUKIN-1B MESSENGER RNA

Authors

David Emergy Skarda, Brigham Young University
Dr. Roger L. Kaspar, Brigham Young University

Keywords

55kD protein, 3'AU-RICH, Interleukin-1B, microbial invasion

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

The polypeptide Interleukin- 1(IL-1) is one of the key mediators of the body’s response to microbial invasion, inflammation, immunological reactions, and tissue injury.1 IL- 1gene expression regulation occurs at many steps. One of the steps currently being researched is translation. Recent research indicates that the translational regulation mechanisms of IL- 1include an AU-rich element in the 3′ untranslated region (Fig. 1).2 In this mechanism, an induced protein binds to the AU-rich element (ARE) causing a decrease in translation efficiency. Isolation and subsequent identification of the ARE binding protein may lead to effective new drugs that induce the ARE binding protein to bind to the mRNA, turning off translation and inhibiting IL- 1gene expression. These drugs could be used to treat pathologies such as diabetes, rheumatoid arthritis, and autoimmune disorders.

Recommended Citation

Skarda, David Emergy and Kaspar, Dr. Roger L. (2013) "ISOLATION OF A 55 kD PROTEIN THAT SPECIFICALLY BINDS THE 3′ AU-RICH ELEMENT OF INTERLEUKIN-1B MESSENGER RNA," Journal of Undergraduate Research: Vol. 2013: Iss. 1, Article 2529.
Available at: https://scholarsarchive.byu.edu/jur/vol2013/iss1/2529