Effects of siRNA-mediated silencing of Phosducin-like Protein Expression on Protein Folding by the Cytoplasmic Chaperonin Complex

Authors

Sarah Warburton, Brigham Young University
Dr. Barry Willardson, Brigham Young University

Keywords

siRNA, phosducin-like protein, protein folding, cytoplasmic chaperonin complex

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

Our lab has recently described an interaction of Phosducin-like protein (PhLP) with the cytoplasmic chaperonin complex (CCT), a sixteen polypeptide complex required for the native folding of actin and tubulin and many other cellular proteins. We found that the binding of PhLP blocked CCT-dependent folding of firefly luciferase in vitro and that over expression of PhLP in Chinese hamster ovary (CHO) cells inhibited actin folding by 80%. Thus, it appears that PhLP is the first known regulator of CCT-dependent protein folding.

Recommended Citation

Warburton, Sarah and Willardson, Dr. Barry (2014) "Effects of siRNA-mediated silencing of Phosducin-like Protein Expression on Protein Folding by the Cytoplasmic Chaperonin Complex," Journal of Undergraduate Research: Vol. 2014: Iss. 1, Article 1133.
Available at: https://scholarsarchive.byu.edu/jur/vol2014/iss1/1133