Bobay Lab

Our group is generally interested in how the specific structure and inherent flexibility of proteins helps them carry out their biological roles. For a few years and with some success, we have been focusing on proteins involved in bacterial response and protection. Proteins responsible for keeping bacteria alive. If you want to see what we're doing in this regard, flip around the website a little and maybe look at a couple of examples of our publications (listed below).

We use NMR as our big platform technology, but we are pretty well-rounded when it comes to addressing our research problems. Consequently some sophisticated mass spectrometry is becoming a major player in our work.

See our major research intersests to the right. Click on them to find a detailed explaination.

Understanding the DNA recognition and binding by the AbrB-like family of transcriptional regulators is of significant interest since these proteins enable bacteria to elicit the appropriate response to diverse environmental stimuli. Although these ''transition-state regulator'' proteins have been well characterized at the genetic level, the general and specific mechanisms of DNA binding remain elusive. We present RDC-refined NMR solution structures and dynamic properties of the DNA-binding domains of three Bacillus subtilis transition-state regulators: AbrB, Abh, and SpoVT. We combined previously investigated DNase I footprinting, DNA methylation, gel-shift assays, and mutagenic and NMR studies to generate a structural model of the complex between AbrBN55 and its cognate promoter, abrB8. These investigations have enabled us to generate a model for the specific nature of the transition-state regulator-DNA interaction, a structure that has remained elusive thus far.

http://news.ncsu.edu/news/2008/11/mkcavanaghstructure.php

All of Dr. Bobay's publications can be found here.

Most Recent 3

Insights into the nature of DNA binding of AbrB-like transcription factors. Bobay BG, Sullivan DM, Kojetin DJ, Thompson RJ, Rance M, Strauch MA, Cavanagh J. Structure. 2008 Nov 12;16(11):1702-13.

Co-evolving motions at protein-protein interfaces of two-component signaling systems identified by covariance analysis. Szurmant H, Bobay BG, White RA, Sullivan DM, Thompson RJ, Hwa T, Hoch JA, Cavanagh J. Biochemistry. 2008 Jul 29;47(30):7782-4.

Targeting RNA with cysteine-constrained peptides. Burns VA, Bobay BG, Basso A, Cavanagh J, Melander C. Bioorg Med Chem Lett. 2008 Jan 15;18(2):565-7