The spliceosome is made up of five riboncucleoprotein particles (snRNPs) and approximately 100 non-snRNP associated proteins that specifically recognize introns and catalyze their removal through two transesterification reactions. I am using both biochemical and biophysical techniques to study these RNA-RNA, RNA-protein, and protein-protein interactions. These interactions are critical because without the correct choice of splice sites, truncated proteins or proteins with the wrong sequence would be produced. Incorrect splice site selection is thought to be responsible for 15% of human diseases.

I am interested in using the deep-sea Pompeii worm, Alvinella pompejana, to isolate pre-mRNA splicing factors because an organism that lives under such extreme conditions (high temperature and pressure) should contain very stable pre-mRNA splicing factors. The use of thermostable proteins or protein/RNA complexes can be very advantageous; for example this allowed the crystal structure of the ribosome to be determined at high resolution. Being included on a research trip to obtain Alvinella pompejana samples and other deep-sea vent eukaryotic organisms will allow me to create libraries (DNA and genomic) and provide material for biochemical characterization such as mass spectroscopy.