We investigate roles and functions of RNA helicases, enzymes that use ATP to bind or remodel RNA and RNA-protein complexes. RNA helicases are structurally highly conserved proteins that are involved in virtually all aspects of RNA metabolism from bacteria to humans: wherever there is RNA in the cell, an RNA helicase is probably there, too. Deregulation or malfunction of certain RNA helicases is linked to numerous diseases, from neurological disorders, to cancer and infectious disease.

Despite their central biological roles, it is not well understood what RNA helicases actually do in the cell. It has become clear that the name “helicase” does not imply that these enzymes just unwind RNA duplexes, but it has remained quite enigmatic what reactions they in fact catalyze. Another puzzling question is the apparent contradiction between the completely promiscuous action of RNA helicases in vitro – they will unwind or bind to essentially any RNA – and their high specificity in the cell – RNA helicases can usually not substitute for one another, despite their high level structural similarity.

Our goal is to understand how RNA helicases physically function in isolation and in the cell. We approach this aim from two sides – by analyzing the enzymatic properties of prototypical RNA helicases in isolation and by determining how these proteins then function in their biological environment. We utilize techniques ranging from molecular biology approaches on yeast along with deep sequencing (RNA-seq) to quantitative biochemical and biophysical methods, including single molecule fluorescence.

Since RNA helicases play central biological roles, our studies have broad implications for understanding the regulation of gene expression, to delineating the cellular response to viral infections.