Rebecca Page, Principal Investigator
Department of Molecular Biology, Cell Biology and Biochemistry
My laboratory uses X-ray crystallography, NMR spectroscopy and small angle X-ray scattering (SAXS) to understand the molecular basis of protein function, with a particular interest in understanding how scaffolding MAP kinases and phosphatases regulate neuronal signaling and T-cell proliferation and how bacterial signaling proteins regulate biolfim formation.Map Kinase Tyrosine Phosphatases
Tyrosine phosphorylation is a key mechanism for the regulation of an extensive set of physiological processes. The KIM phosphatases, including hematopoietic tyrosine phosphatase (HePTP), bind MAP kinases through a unique targeting mechanism which results in the reciprocal regulation of one another’s biological activities. We are interested in understanding the molecular basis for the reciprocal regulation of the KIM phosphatase:MAP kinase interactions to determine how these interactions are modulated and directed by multiple kinase signaling pathways in the cell.
Bacterial Biofilms
In recent years, genes important for E. coli biofilm formation and propagation have been identified using DNA-array experiments, proteome analysis, and classical knockout studies. Identified genes code for proteins involved in bacterial motility, quorum sensing, and the induction of polysaccharide synthesis. Unfortunately, the specific biochemical functions of many of these genes are unknown. Because protein function is more highly correlated with structure versus sequence, we are using X-ray crystallography and NMR spectroscopy to determine the atomic resolution structures of these proteins and protein complexes to gain insights into their individual and coordinated functions in antibiotic resistance resulting in a protein biofilm interaction network map.
Graduate student Dana Francis received an IUCR Travel Award to attend the IUCR Congress in Madrid in August. (4/2011)
Graduate student Dana Lord was selected to attend RapiData 2011 where she solved two crystal structures. (4/2011)
Undergraduate student Jennifer Arruda was selected as the local ACS chapter student of the year. (4/2011)
The 2nd annual Protein Science Workshop, a collaboration between the Page lab and the Biotechnology Certificate Program at CCRI was held. (3/2011)
Graduate student Dorothy Koveal received a Keystone Fellowship to present her research at the 'Frontiers of NMR in Biology'.(1/2011)
Lutz Tautz, Ph.D., The Burnham Institute.
Thomas Wood, Ph.D, Texas A&M University.
For a full publication list, click here.
Wang et al (2011) Antitoxin MqsA helps mediate the bacterial general stress response Nat Chem Biol. [Epub ahead of print]
Brown et al (2011) Structure of the Escherichia coli antitoxin MqsA (YgiT/b3021) bound to its gene promoter reveals extensive domain rearrangements and the specificity of transcriptional regulation. J Biol Chem 286: 2285-2296.