First name,Last name,Preferred title,Overview,Position,Department,Individual
Timothy,Devarenne,Associate Professor,"We study the biochemical and molecular mechanisms underlying the control of programmed cell death (PCD) in plants and how PCD is manipulated during plant-pathogen interactions. Specifically we study the interaction between tomato and Pseudomonas syringae pv. tomato (Pst) the causative agent of bacterial spot disease. Resistance to this disease is conferred by the host Pto serine/threonine protein kinase which recognizes Pst strains expressing the type III effector protein AvrPto.
PCD is induced during both resistant and susceptible plant-pathogen interactions. In the case of a resistant interaction, PCD induced by the plant, known as the hypersensitive response (HR), and acts to limit the spread of the pathogen. In susceptible plant-pathogen interactions plant PCD is induced by the pathogen after infection leading to death of the host. Studies have indicated that the genes controlling host PCD during the HR are the same genes that are manipulated by the pathogen during susceptible interactions. The difference lies in the timing of controlling the activity of these genes; HR PCD occurs within 12 hours of pathogen recognition while pathogen-induced PCD occurs several days after infection.
Many of these genes that control plant PCD are serine/threonine (S/T) protein kinase. We are interested in studying a specific class of S/T protein kinases that control PCD in plants called AGC kinases and how they are regulated in both resistant and susceptible plant-pathogen interactions. Additionally, when plants are not attacked by pathogens, PCD is a process that requires constant control so that cell death does not occur. We are looking at the signaling mechanisms and pathways employed to keep PCD under check in non-pathogen challenged plants.",Faculty Affiliate||Associate Professor,Energy Institute||Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n11411275
Xiuren,Zhang,Professor,"Our laboratory focuses on systemic analysis of biochemical, molecular and biological functions of AGO family proteins (AGOs-mics) in genetically tractable Arabidopsis and economically important crops (i.e. rice). We'd like to identify the small RNAs, mRNA targets and protein components which associate with these AGOs. We will study protein/RNA and protein/protein interactions in these RISC assembly events. Our goal is to understand how these AGOs are functionally specialized or redundant corresponding to endogenous development cues and external environmental stimuli. Particularly, we'd like to learn how plants reprogram their gene expression through the small RNAs and AGOs to construct a new cellular niche in responses to environmental challenges and biotic stresses.
Another aspect of our research involves host/virus interaction. Plants take advantage of RNA silencing pathways to defend themselves from exogenous nucleic acid invaders (i.e. viruses). As an anti-host defense mechanism, viruses encode suppressors that can block RNA silencing responses. We have recently demonstrated that CMV 2b disables AGO1 cleavage activity to inhibit RNA silencing and to counter host defense. We are now extending our study to suppressors of several other viruses and the molecular mechanisms of their suppression.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n220933ad
Paul,Straight,Associate Professor,"Our goal is to understand how microorganisms interact in complex communities. Specifically, we study how small molecules produced in a microbial community affect the growth, development and metabolic output of the organisms. We use a combination of microbiology, genetic, genomic, and biochemical approaches to dissect complex interspecies interactions. Currently, our research focuses on the interactions of the soil bacteria Bacillus subtilis and members of the genus Streptomyces, known for their prolific production of bioactive small molecules and development of aerial structures and spores.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n5540637b
Margaret,Glasner,Associate Professor,"Evolution is the organizing principle of biology and provides the cornerstone of our approach to understand the relationships between protein structure and function. We combine bioinformatics, biochemistry, and genetics to address fundamental questions about protein evolution, such as: What structural and mechanistic features of enzymes increase their capacity to evolve new functions? How do new metabolic pathways evolve? Are there multiple evolutionary pathways to evolve new enzyme activities?
Our primary focus is on how catalytic promiscuity serves as the raw material for evolving new enzyme activities. Catalytic promiscuity is the ability to catalyze different chemical reactions using the same active site. Many enzymes in one branch of the protein family we are studying are catalytically promiscuous, and this activity has been incorporated into new metabolic pathways more than once. Comparing the sequences and structures of these proteins will identify characteristics that permitted them to evolve the second activity.
Our goal is to use results from our research to identify fundamental evolutionary principles that can can help decipher protein structure-function relationships, predict protein functions, and improve protein engineering methods.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/n721200c3
Hays,Rye,Associate Professor,"A fundamental principle of biology is the use of chemical energy in the form of ATP to assemble, disassemble and alter macromolecular structure. Specialized control proteins known as molecular chaperones are often responsible for this activity and have been recognized in recent years to be essential for regulating many aspects of cellular biology. Using a variety of biophysical and biochemical techniques, the Rye lab focuses on three fundamental cellular processes that require molecular chaperones: (1) protein folding (2) protein disaggregation and (3) vesicle trafficking. In each of these cases, large quantities ATP are burned, resulting in molecular organization in the case of protein folding, and molecular disassembly and remodeling in the case of protein disaggregation and vesicle trafficking. We are interested in understanding the detailed biophysical mechanisms that underpin these events. Why are these processes so energetically expensive? Are there any similarities in how the energy is used between these very different molecular processes? Are there general principles of energy transduction in biology that can be gleaned by comparing these examples with other molecular machines, such as cytoskeletal motors? Understanding how molecular chaperones control protein and membrane organization will provide key insights into not only basic cell biology, but will also illuminate aspects of many diseases that spring from aberrant protein and membrane dynamics.",Associate Professor,Biochemistry and Biophysics,https://scholars.library.tamu.edu/vivo/display/ne7fb85e1