Analysis of eIF4E1 Conservation and Synteny across Drosophila Species to Understand the Evolution of the Insulin Pathway
Authors: Jessica Strand; Jami Feist; Emma Sirjord; Sydney Payeur; Breanna Hoffman; Paula Croonquist
Affiliation: Anoka Ramsey Community College
Keywords: a. genome evolution; n. other (Bioinformatics )
The Insulin/Tor signaling pathway regulates important physiological functions such glucose and lipid metabolism, cell growth and survival. It is highly conserved from fruit flies to mammals. This pathway is also critical for homeostasis and its dysregulation results in prevalent human diseases such as in Type II Diabetes, Cardiovascular disease and even cancer. The eukaryotic translation initiation factor 4E1 (eIF4E1) encodes for a member of the eIF4F cap-binding complex that is required for cap-dependent translation of mRNA. The purpose of this study was to determine the conservation of the eIF4E1 gene in multiple species of Drosophila relative to D. melanogaster. It was hypothesized that the species highly divergent from the reference species would exhibit less eIF4E1 conservation than those closely related to the reference species. It was predicted that this gene would be most conserved in D. serrata and least conserved in D. arizonae. Gene models were proposed utilizing the UCSC Genome Browser, BLAST, Flybase gene record finder and verified by Gene Model Checker. The synteny analysis and protein alignments observed suggest that eIF4E1 in D. takahashii is the most conserved and D. arizonae is the most divergent. However, all five species had a high eIF4E1 protein identity ranging 81-94%. Previous evidence has demonstrated that position in the insulin signaling pathway may affect selective constraint, with downstream genes evolving at a slower rate than genes closer to the membrane. This may explain the high level of conservation for the eIF4E1 gene. Further studies should aim to investigate the impact of position, connectivity and/or other factors shown to influence this pathway’s selective constraint.