Off-campus University of Richmond users: To download campus access theses, please use the following link to log in to our proxy server with your university username and password.
Date of Award
Restricted Thesis: Campus only access
Bachelor of Science
Biochemistry & Molecular Biol.
Ded1 is an ATP-dependent RNA helicase implicated in translation initiation. Ded1 is known to be required for the resolution of highly structured 5' UTRs in order for the 48S pre-initiation complex to bind and scan for the start codon. Ded1 has two roles in translation initiation. First, Ded1 assembles with eIF4F during mRNA activation to prime the mRNA. Then, Ded1 uses its ATP-dependent helicase activity to unwind the secondary structure of the 5'UTR and resolve barriers along the mRNA. It was previously found that Ded1 is methylated at four arginine residues (Erce et al., 2013). In this paper, the effect of methylation on Ded1 protein is evaluated through in vitro translation, with future plans to perform helicase assays and oligomerization assays
Murvin, McKenzie, "The effects of arginine methylation on the function of Ded1, an RNA helicase, in vitro" (2019). Honors Theses. 1414.