Interests (science):
In the lab I study posttranslational modifications in prokaryotes. I am always interested in how things work (biochemistry) and why they work (physiology).

Interests (non-science):
I am from Wisconsin so here is my beer, cheese, brats, and Packers plug. I also enjoy cross-stitching, sewing, weight-lifting, getting to know people, going to Aldi, gardening, hammock relaxing, going to downtown Athens on a sunny day, eating, and did I mention cheese?

Protein Specificity: How do different acetyltransferases with conserved active sites recognize their diverse substrates?

Acetyltransferases catalyze the transfer of an acetyl group to α or ε groups of proteins and to amine groups of small molecules. A single organism can encode 20-70+ acetyltransferases, all of which are hypothesized to have different substrates. These acetyltransferases have highly conserved structures, yet each acetyltransferase can only recognize and acetylate a certain protein or small molecule. My research focuses on studying the structural specificity of acetyltransferases and how this extremely conserved family of proteins can target such diverse substrates.  

Posttranslational modifications: How does reversible lysine acetylation play a role in bacterial physiology?

Rhodopseudomonas palustris has one of the best-studied systems for photoheterotrophic benzoate degradation. The genes encoding the benzoate-degrading enzymes are clustered and fully characterized, with the exception of a putative acetyltransferase encoded by badL. My work aims at determining the role of BadL in benzoate degradation and to advance our understanding of acetylation in cell physiology.