Date of Award


Degree Type


Degree Name

Master of Science in Biological and Environmental Sciences (MSBES)


Cell and Molecular Biology


Cell & Molecular Biology

First Advisor

Steven Gregory


Ribosomes are macromolecular machines that are responsible for protein synthesis and are a central component of gene expression. They are made up of ribosomal RNA and ribosomal proteins organized into two subunits; the 50S subunit, containing 23S and 5S rRNA and around 33 ribosomal proteins, and the 30S subunit, containing of 16S rRNA and around 21 ribosomal proteins. All of these components are created in stochiometric amounts and combine to assemble into the structure of the ribosome. Ribosome assembly is a large investment of energy by the cell, which has to create tens of thousands of ribosomes accurately and efficiently. A great deal is known about how the ribosome functions during protein synthesis, while less is known about how it assembles. Current models for assembly propose that the primary role of ribosomal proteins is to accelerate proper folding of the rRNA into its functionally active conformation and to prevent the formation of kinetically trapped, misfolded RNA intermediates.

The overall goal of this project was to investigate the role of a specific ribosomal protein, uS17, in establishing the tertiary structure of the 30S subunit. Ribosomal protein uS17 is a highly conserved component of the 30S subunit that plays a key role in its assembly. It is a primary binding protein that binds directly to 16S rRNA in the absence of other proteins. Deletion of the gene encoding uS17 causes a subunit assembly defect, leading to a severe growth deficiency and a temperature sensitive phenotype. The current study is based on a uS17 knockout strain of T. thermophilus strain HB27, which was used to investigate the role of uS17 in 30S ribosomal subunit assembly.



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