Date of Award

1-1-2022

Language

English

Document Type

Master's Thesis

Degree Name

Master of Science (MS)

College/School/Department

Department of Biological Sciences

Content Description

1 online resource (v, 34 pages) : illustrations (some color)

Dissertation/Thesis Chair

Gabriele Fuchs

Committee Members

Cara T Pager, Alex M Valm

Keywords

lysine acetylation, lysine acetyltransferase, poliovirus, ribosomal protein, Ribosomes, Poliovirus, Betaine, Acetylation

Subject Categories

Molecular Biology | Virology

Abstract

Ribosomes have been traditionally viewed as invariable machinery, but in recent years more and more evidence for their heterogeneity has emerged. Core ribosomal proteins, ribosomal-associated proteins, and post-translational modifications all contribute to the variations found within these crucial subcellular components.In our research, we focused on lysine acetylation – a post translational modification found on many ribosomal proteins. We used a chemical inhibitor of acetyltransferases KAT 3A and KAT 3B to observe the effect that inhibiting acetylation may have in the context of translation. By using poliovirus to shut off conventional cellular translation, we were able to look at a narrow slice of translation – namely, IRES-mediated viral translation in response to acetylation inhibition. We used a combination of experiments, from plaque assays for broader phenotypic observation of KAT3 inhibition, to DNA and RNA transfections, and 35S metabolic assays for a closer focus on specific aspects of the viral life cycle.

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