U1A-RNA Complex formation: Insights from combining experimental and computational approaches

COMP 30

Anne M. Baranger, baranger@uiuc.edu, Department of Chemistry, University of Illinois, School of Chemical Sciences, 600 S. Mathews Ave., Urbana, IL 61801
RNA-protein complexes are essential contributors to many important biological processes, including gene expression. An understanding of how proteins recognize RNA is needed to describe and control processes involving RNA-protein complexes. We are investigating the recognition of RNA by a set of proteins that contain an RNA recognition motif (RRM), which is one of the most common RNA-binding domains. The focus of this study is a particularly well-characterized system, the complex formed between the N-terminal RRM of the U1A protein and stem loop 2 of U1 snRNA. We have investigated the binding and dynamics of wild type and mutant U1A proteins and stem loop 2 RNAs using both experimental and computational approaches in order to understand and predict local and long-range energetic contributors to binding affinity and specificity. We have focused in particular on the roles highly conserved aromatic amino acids play in determining complex stability.