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Date of Award

2015

Document Type

Restricted Thesis: Campus only access

Degree Name

Bachelor of Science

Department

Biochemistry & Molecular Biol.

First Advisor

Dr. Angela Hilliker

Abstract

In order to regulate protein expression, mRNAs are constantly shifting from translation to translation repression or degradation. All mRNAs associate with proteins that regulate the fate of the mRNA in ribonucleoprotein (RNP) complexes. Translating mRNAs interact with the ribosome and proteins necessary for each step of translation, and mRNAs that will be degraded associate with proteins that signal for this degradation. Repressed mRNP complexes can aggregate in cytoplasmic foci, such as processing (P) bodies and stress granules (SGs), which are highly conserved among eukaryotic organisms. These aggregates are especially prevalent during times of stress to the cell, when fewer mRNAs are translated to conserve energy. Although P- bodies and SGs contain different sets of proteins, the protein composition of mRNA storage granules is dynamic (Fig. 1) and granules can form with components of both P-bodies and SGs depending on the condition of the cell (Kedersha et al., 2005; reviewed in Buchan and Parker, 2009). Both types of mRNA storage granules form as a result of translation inhibition; however, P-body formation is a normal part of the life of a cell that can be aggravated by cellular stresses, while SGs only form in response to translation initiation inhibition (Kedersha et al., 1999; Teixeira et al., 2005; Shah et al., 2013). Both P-body and SG formation is dependent on the amount of non-translating mRNAs in the cell (Teixeira et al., 2005; Hoyl et al., 2007); therefore, these structures are useful markers of non-translating mRNAs.

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