DDis3 N-Terminus Terminal Domains and RNA Metabolism Interactions
A respected investigator in RNA biology and transcriptional research, Erik Andrulis, PhD, most recently held a position with Case Western Reserve University as assistant professor. While at Case Western, Erik Andrulis published an important paper in the peer-reviewed journal Nucleic Acids Research entitled, “Drosophila Melanogaster Dis3 N-Terminal Domains Are Required for Ribonuclease Activities, Nuclear Localization and Exosome Interactions.”
With eukaryotic cells employing a variety of pathways in regulating RNA localization, production, and stability, a number of these are under the control of ribonucleases such as Dis3. Though Dis3 was known to be an essential ribonuclease in defining RNA metabolic pathways, the enzyme’s role had not been well defined in the areas of interaction with the eukaryotic RNA exosome and subcellular localization.
Andrulis and his colleagues set in place a set of Drosophila melanogaster Dis3 (dDis3) mutants and evaluated their in vitro enzymatic activity, as well as their S2 tissue culture cell localizations and interactions. Study findings included that the dDis3 N-terminus is sufficient for endoribonuclease activity to occur in vitro. A proper N-terminal domain structure plays a critical role in enabling full-length polypeptide activity. These and other data suggest that the dDis3 N-terminus serves as a complex, dynamic hub for exosome and RNA metabolism interactions.