Sciences and Mathematics, College of
Biology, Department of
BURS Faculty Advisor
In eukaryotic cells, such as the budding yeast Saccharomyces cerevisiae, mRNA export is the essential process in which mature mRNA is transported from its site of production, the nucleus, through the nuclear pore complex (NPC) to the cytoplasm, where it can then be translated into protein. This is accomplished when a transcript interacts with the mRNA export protein Mex67, which shuttles the message across the NPC. When the cell is under conditions of stress, such as heat shock, most mRNA export is prohibited to allow for selective gene expression for cell recovery. However, some transcripts are able to be selectively exported and expressed in these conditions. An example is SSA4, which encodes a protein that assists denatured proteins to refold under stress conditions and is up-regulated in response to heat shock. It is not known how SSA4 is selectively exported from the nucleus. I hypothesize that an unknown adaptor protein binds to the SSA4 transcript to recruit Mex67. To test this hypothesis, we will perform a yeast three-hybrid (Y3H) test by constructing a plasmid which contains the SSA4 ORF and 3’ UTR, in addition to MS2 hairpins. This construct will be assessed for interaction with Mex67. If no interaction is observed, then we will perform a screen for other proteins that are able to interact with the SSA4 transcript.
Stalnaker, Gretchen E. and Adams, Rebecca, "Analyzing Mex67 Interaction with the SSA4 Transcript for Selective Export" (2023). Belmont University Research Symposium (BURS). 236.