My laboratory studies two processes. The first is the ubiquitin pathway, which is a protein modification pathway, whereby the protein ubiquitin is covalently attached to other proteins. This alters the longevity, activity or localization of the ubiquitinated protein. We are interested in understanding the specificity and regulation of the ubiquitin pathway. We try to understand how proteins are recruited to the ubiquitinating enzymes. There are are large number of ubiquitinating enzymes whose functions are not known. We are taking a reverse genetics approach to understand the function of RING E3 ligases which interact with substrate proteins and catalyze ubiquitin transfer. We use a variety of techniques- biochemistry, molecular biology and genetics.
We also study a family of proteins called pfkB proteins, proteins related to E. coli phosphofructokinase, but which have diverse and uncharacterized roles. We are focusing on a subset of pfkB proteins localized to the plant plastid. Some of these are important for chloroplast transcription and we are determining their functions.
