Science University Research Symposium (SURS)


Analysis of Gle1 Stimulating Dbp5 Activity

Publication Date



Sciences and Mathematics, College of


Chemistry and Physics, Department of

SURS Faculty Advisor

Rachel Rigsby

Presentation Type

Poster Presentation


The mRNA nuclear export process is a tightly regulated biological system important for eukaryotic gene expression. While the mRNA is sequestered inside the nucleus, the transcript associates with a protein, Mex67, to be transported through nuclear pore complexes (NPCs) out of the nucleus and into the cytoplasm, the site of translation. In the cytoplasm, Mex67 is removed from the transcript, which is facilitated by the binding of the protein complex Dbp5-ATP, Gle1, IP6, and Nup42. Gle1 stimulates ATPase activity of Dbp5, which enables binding to the transcript and catalyzing the hydrolysis from ATP to ADP, ultimately releasing mRNA for the proteins to be recycled. Therefore, knowing the extent at which Gle1 stimulates Dbp5 ATPase activity is essential for successful mRNA export. Throughout this study, a biochemical system was used to ensure optimized induction of MBP-Gle1 in E. coli Rosetta cells. Other efforts of the system included sonicating the induced cells for successful extraction of Gle1, which will be purified for in vitro analysis. The ultimate goal of this project is to obtain purified Gle1 in order to determine how it affects Dbp5 activity.

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