Ubiquitin-like proteins (Ubls) are conjugated to target proteins or lipids to regulate their activity, stability, subcellular localization, or macromolecular interactions. Conjugation is achieved through a cascade of activities that are catalyzed by E1 activating enzymes, E2 conjugating enzymes, and E3 ligases. We are focused on understanding how Ubl conjugation pathways achieve selectivity for particular targets, and how conjugation generates signals in processes ranging from DNA repair to the cell cycle.

RNA quantity and quality are regulated by a balance between transcription and degradation. We have focused on characterizing the activities of the RNA exosome, an essential multi-subunit protein complex that catalyzes 3' to 5' process or decay of nearly every class of cellular RNA in the nucleus and cytoplasm.

Past interests of the laboratory included studies to address RNA processing and repair as well as antioxidant defense pathways in Mycobacterium tuberculosis.