We have recently published a combination of biophysical and biochemical studies of the N-terminal PAS-A domain from B. subtilis KinA, a sensor histidine kinase which regulates sporulation. In Lee et al., 2008 (selected as a Biochemistry Hot Article, we demonstrate that PAS-A adopts a stable homodimer in isolation. Point mutations at the dimerization interface can either activate or inhibit kinase activity, both in vitro and in vivo. Given the widespread use of PAS domains as sensory modules in this class of bacterial kinase, our data provides support for potential regulatory models.

We've also recently published two reviews: one of the role of PAS domains in hypoxia inducible factor (HIF), the other on the outstanding graduate program in Molecular Biophysics at UT Southwestern.