Xiphophorous LARP6 La Motif: To Bind or not to BindIdaho Conference on Undergraduate Research
Acknowledgement of Funding SourcesThe project described was supported by the Pacific Northwest Louis Stokes Alliance for Minority Participation through the National Science Foundation under Award No. HRD-1410465 and Institutional Development Awards (IDeA) from the National Institute of General Medical Sciences of the National Institutes of Health under Grant No. P20GM103408. We also acknowledge support from The Biomolecular Research Center at Boise State with funding from the National Science Foundation, Grant Nos. 0619793 and 0923535, the MJ Murdock Charitable Trust and the Idaho State Board of Education.
AbstractFibrosis is a serious disease that causes extra deposition of connective tissue that can lead to loss of function of a given system in the human body. The main protein found in fibrotic tissues is Type I collagen. The type I collagen mRNA is synthesized in the nucleus and transferred to the rough ER with the help of LARP6. The major mRNA binding domains found in LARP6 are the La Motif (LaM) domain and an (RNA Recognition Motif) RRM domain. We hypothesize that if we can disrupt the binding activity of LARP6 with type I collagen mRNA, then we can disrupt the synthesis of the type I collagen protein. Understanding how LARP6 interacts with mRNA will inform drug design efforts that can help reduce or eliminate fibrosis. Here, we optimized protein expression in an E. coli platform to produce isotope enriched LaM for Nuclear Magnetic Resonance (NMR) studies. NMR spectra will be used to map the RNA binding surface onto LARP6 LaM and to compare structural features between LARP6s from different species. This information we help us to better understand the LaM domain in LARP6.
Citation InformationRafael J Gomez and Lisa Warner. "Xiphophorous LARP6 La Motif: To Bind or not to Bind"
Available at: http://works.bepress.com/lisa-warner/26/