The Conservation of The GlyP Gene Across highly divergent species of Drosophila
Authors: Bethany Lieser; Reece Lawlor; Bao Khang; Alyssa Beise; Paula Croonquist
Affiliation: Anoka-Ramsey Community College
Keywords: a. genome evolution; n. other (Bioinformatics)
The Insulin/Tor signaling pathway is responsible for the uptake of glucose into cells and its metabolism. It has also been linked to cell growth, fat and protein metabolism, and longevity. Its dysregulation in humans plays a major role in Type II Diabetes, Cardiovascular Disease, and cancer. GlyP, a member of the Insulin signaling pathway, encodes for the glycogen phosphorylase enzyme which is responsible for glycogen breakdown in the cell by releasing glucose into the bloodstream. Previous evidence has indicated that a gene’s selective constraint is influenced by its protein connectivity and position in pathway, among other factors, so that genes with less molecular interactions and a closer location to the membrane evolve faster than those with more protein-protein interactions and located closer to the nucleus. We hypothesized that GlyP would exhibit high selective constraint in D. busckii, D. hydei, D. kikkawai, and D. suzukii when compared to D. melanogaster, the reference species, due to its high connectivity and downstream position in the insulin pathway. The GlyP gene was annotated in each species utilizing the Genomics Education Partnership (GEP) tool pipeline, namely, the UCSC Genome Browser, tBlastn, Blastp, the Gene Record Finder, and verified in the Gene Model Checker. Genes models were proposed based on synteny, RNAseq data and other lines of evidence. The protein alignment of GlyP in all species was examined. All species were within 97% similar to the reference species despite D. busckii being the furthest diverged species from D. melanogaster. This supports our hypothesis that highly connected genes, also known as hubs, are under high selective constraint even in species vastly separated by evolutionary time. The gene’s downstream position may also provide evidence that GlyP is highly conserved and a cornerstone enzyme in the insulin pathway.