Area of Doctoral Study: Pharmaceutical Science
Undergraduate Institute: Xavier University of Louisiana
Research Advisors: Sarah Michel, Ph.D.
Description of Research
Zinc finger (ZF) proteins utilize zinc as a structural co-factor to fold and function. ZF functions range from the regulation of transcription (via DNA binding) to translation (via RNA binding). More than 10% of the human genome encodes for ZF type proteins, yet many of these ZFs’ mechanisms of metal mediated DNA, RNA or protein recognition are poorly understood. Our laboratory is interested in understanding the mechanisms of metal mediated DNA and RNA recognition by new, ‘non-classical’ classes of ZFs. ZFs under study by our laboratory include tristetraprolin (TTP) and cleavage and polyadenylation specificity factor 30 (CPSF30). TTP plays an important role in regulating inflammation, and current efforts in the laboratory are focused on understanding how exogenous metals affect TTP function and translating biochemical findings to cellular activity. CPSF30 is part of a complex of proteins that regulate pre-mRNA. Our laboratory was the first to isolate this protein, and we discovered that it contains a 2Fe-2S co-factor, in addition to Zn. Current efforts are focused on understanding the functional role of the 2Fe-2S co-factor, as well as the mechanism of RNA recognition.