Date of Award

12-21-2020

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

School of Biological Sciences

First Advisor

Christopher S. Weitzel

Abstract

An ancient and ubiquitous set of enzymes known as the aminoacyl-tRNA synthetases are required for the viability of all organisms. The aminoacyl-tRNA synthetases catalyze the attachment of amino acids onto tRNA molecules. The aminoacylated, or charged, tRNA is then transported and utilized at the ribosome for the synthesis of proteins. The genome of the hyperthermophilic microorganism Sulfolobus islandicus (S. islandicus) harbors a unique leucyl-tRNA synthetase paralog, LeuRS-I, of unknown function. While its duplicate, LeuRS-F, carries out all the classical functions of LeuRS-family enzymes, LeuRS-I fails to charge leucine onto tRNALeu, despite its ability to activate this amino acid and bind this tRNA substrate. To begin to understand the molecular function of this unusual LeuRS within S. islandicus, new approaches of inquiry are needed. A variety of biotechnological methods were developed in an attempt to piece together the activity of this paralogous synthetase and understand the role it plays within S. islandicus.

Comments

Imported from Bretz_ilstu_0092N_11845.pdf

DOI

https://doi.org/10.30707/ETD2021.20210719070603170967.93

Page Count

111

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