Abstract
Transmission of genetic information from DNA to protein passes through a messenger‐RNA intermediate. This mRNA is extensively processed after transcription, and one enzyme that does so is adenosine de aminase that acts on RNA (ADAR). ADARs catalyze the deamination of adenosines into inosines on double‐stranded RNA (dsRNA) substrates, ultimately leading to a mutation in their encoded protein. These mutations are essential not only for a properly functioning nervous system, but for survival. The ADAR enzyme is composed of two domains: a catalytic domain and an RNA binding domain that consists of one or more double‐stranded RNA binding motifs (dsRBMs). Determining the structures of these dsRBMs could lead to insight on the substrate specificity observed in ADARs, as it is known they are not sequence specific. To do so, dsRBMs from various organisms were subcloned into an expression plasmid, expressed, purified, re‐folded, and will be crystallized to determine their 3D structure by X‐ray diffraction. The structures of these dsRBMs from different organisms will be compared for similarities and differences to gain understanding into the mechanism by which they recognize their specific substrates.Support or Funding InformationButler Summer Institute (CLB, Summer 2019)Holcomb Awards Committee Grant (MRM, 2019)
Published Version
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