Date of Award:


Document Type:


Degree Name:

Master of Science (MS)


Chemistry and Biochemistry

Committee Chair(s)

Sean J. Johnson


Sean J. Johnson


Ryan N. Jackson


Joan M. Hevel


The central dogma of biology states that DNA is transcribed into RNA, which is translated into protein. However, this concept portrays RNA purely as an intermediary step from DNA to protein. RNA plays an essential and vital role in a cell, including; regulating protein and RNA levels, act as a template for protein synthesis, cell differentiation, regulatory processes, and signaling molecules. If cells do not adequately monitor and regulate RNA levels, it can lead to disease states and even cell death. The main protein complex that regulates the maturation and degradation of RNA in the nucleus is the RNA nuclear exosome. The nuclear exosome requires an essential cofactor to be active, the RNA helicase Mtr4.

Mtr4 unwinds structured or double-stranded RNA to feed a clean single-stranded RNA to the nuclear exosome for trimming or degradation. By understanding how Mtr4 interacts with its RNA substrates, we can advance our fundamental knowledge on how our cells regulate RNA. In this thesis, a detailed analysis of the novel arch domain of Mtr4 is investigated. We look at the mobility of the arch domain, what RNA characteristics it prefers to bind, and the role of the arch domain in helicase activity.



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