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Barrett, The Honors College at Arizona State University proudly showcases the work of undergraduate honors students by sharing this collection exclusively with the ASU community.

Barrett accepts high performing, academically engaged undergraduate students and works with them in collaboration with all of the other academic units at Arizona State University. All Barrett students complete a thesis or creative project which is an opportunity to explore an intellectual interest and produce an original piece of scholarly research. The thesis or creative project is supervised and defended in front of a faculty committee. Students are able to engage with professors who are nationally recognized in their fields and committed to working with honors students. Completing a Barrett thesis or creative project is an opportunity for undergraduate honors students to contribute to the ASU academic community in a meaningful way.

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Expression and Purification of the Telomerase RNA Binding Domain of Telomerase Reverse Transcriptase from Purple Sea Urchin (Strongylocentrotus purpuratus)

Description
Telomerase is a reverse transcriptase that is responsible for the addition of telomeric repeats on to the ends of eukaryotic chromosomes. The purple sea urchin, Strongylocentrotus purpuratus, telomerase enzyme is unique in that its telomerase RNA does not contain the ancestrally conserved CR4/5 domain and instead contains the functionally equivalent…

Telomerase is a reverse transcriptase that is responsible for the addition of telomeric repeats on to the ends of eukaryotic chromosomes. The purple sea urchin, Strongylocentrotus purpuratus, telomerase enzyme is unique in that its telomerase RNA does not contain the ancestrally conserved CR4/5 domain and instead contains the functionally equivalent eCR4/5 domain. Binding between the purple sea urchin TRBD and eCR4/5 domain is currently poorly understood due to eCR4/5's unique structure. In this work the telomerase RNA binding domain, TRBD, of the purple sea urchin telomerase reverse transcriptase, TERT, was fused to maltose binding protein (MBP) using several different short amino acid linkers and purified via amylose column purification. Short amino acid linkers were cloned into the MBP sea urchin TRBD constructs to facilitate better crystallization of the fusion protein. Future work of this project includes testing telomerase RNA binding affinity to the TRBD constructs and determining the crystal structure of the sea urchin TRBD with bound eCR4/5. Elucidating how eCR4/5 binds to the sea urchin TRBD will provide insights into the evolutionary relationship between eCR4/5 and the pseudoknot/template domain of sea urchin telomerase RNA.
ContributorsKing, Robert (Author) / Chen, Julian (Thesis director) / Li, Yang (Committee member) / Barrett, The Honors College (Contributor)
Created2018-05