Title: Associate Professor
Other Departments: Biochemistry
Degrees: B.S. (Chemistry), Florida International University; Ph.D. (Biological Chemistry/Biophysics), University of North Carolina at Chapel Hill
Office Location: Doane Hall of Chemistry C.015
Office Hours: M 8-9 am; T 10:45 am-12 pm; W 1:30-2:30 pm; F 8-10:30 am, 1:30-2:30 pm
RNA plays a crucial structural and catalytic role in a variety of important cellular processes. They are synthesized as single-stranded chains and must fold into defined complex structures, like proteins, to accomplish their diverse functions. Structural versatility is a challenge for most RNAs due to the difficulty of reaching the native folding state. Hence, protein cofactors are usually necessary to stabilize or modulate RNA folding. One type of RNA protein cofactors are the ubiquitous DEAD-box proteins. DEAD-box proteins are essential in all aspects of RNA metabolism including pre-mRNA splicing, ribosome biogenesis, RNA interference, translation, mRNA transport, and decay. These motor proteins modulate RNA-RNA, RNA-protein, and/or protein-protein interactions by utilizing nine conserved motifs to convert RNA binding and ATP hydrolysis into distinct conformational changes. As part of the helicase superfamily 2 (SF2), DEAD-box proteins are formally putative RNA helicases. However, ATP driven unwinding of RNA duplexes has only been illustrated for few proteins. The main focus and motivation of my research has been to biochemically understand the structural interactions and the role that proteins play in RNA catalysis and folding in eukaryotic RNA metabolism.