First name,Last name,Preferred title,Overview,Position,Department,Individual
Leland,Pierson,Professor and Head,,Professor and Head,Plant Pathology and Microbiology,https://scholars.library.tamu.edu/vivo/display/n4162e884
Thomas,Mcknight,Professor and Head,"My lab is currently investigating mechanisms that regulate telomerase activity in plants. We previously showed that the pattern of telomerase expression in plants is remarkably similar to the pattern seen in humans, despite fundamental differences in development between plants and animals. Telomerase is abundantly expressed in reproductive organs but is undetectable in most vegetative organs (Fitzgerald et al., 1996). Additionally, telomerase can be induced in leaves and other vegetative organs by exposure to exogenous auxin.
To isolate genes that regulate telomerase, we screened a large population of activation tagged lines of Arabidopsis thaliana, and found that several lines that ectopically express telomerase in leaves. The first line we characterized over-expressed a gene encoding a small zinc finger transcription factor we designated TELOMERASE ACTIVATOR 1 (Ren et al., 2004). This factor does not bind to the promoter for TERT, which encodes the catalytically active subunit of telomerase. Instead, it binds to and activates transcription of BT2, a gene encoding a component of a ubiquitin ligase (Ren et al., 2007). Our working model is that the BT2 ubiquitin ligase marks a telomerase repressor for destruction, thereby allowing expression of telomerase. Efforts in the lab are currently focused on identifying the presumed telomerase repressor protein and other proteins that interact with BT2.",Professor and Head,Biology,https://scholars.library.tamu.edu/vivo/display/n5c3b294a
Jonathan,Levine,Professor and Head,,Professor and Head,Small Animal Clinical Sciences,https://scholars.library.tamu.edu/vivo/display/n8ae2a0a7
Gregory,Reinhart,Professor and Head,"Our laboratory is interested in the mechanisms by which enzymes are regulated in the cell. In particular, we are interested in allosteric regulation of enzyme activity. Consequently, we are interested in understanding the nature of the conformational change in proteins that can be effected by the binding of ligands, and specifically how these changes alter the catalytic behavior of enzymes subject to allosteric regulation. We endeavor to investigate properties that are complementary to those determined by x-ray crystallography in order to develop a comprehensive picture of the structure-function relationships involved in the regulatory phenomenon. For example, we are interested in how the dynamics of protein structure might dictate the nature of an allosteric effect. Techniques and approaches that we use in the laboratory include analysis of enzyme kinetics; analysis of the thermodynamics of enzyme-ligand interactions; time-resolved and steady-state fluorescence spectroscopy; analysis of the effects of temperature and hydrostatic pressure (up to 4 kbar) on enzyme properties, site-specific mutagenesis, isothermal titration calorimetry, and molecular graphics.",Professor and Head,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/na6e2a0db