Tamara L. Hendrickson
Tamara L. Hendrickson
Research interest(s)/area of expertise
GPI membrane anchoring of proteins, indirect tRNA aminoacylation, accuracy mechanisms in protein biosynthesis, membrane proteins, protein-protein interactions, enzyme kinetics
Our research group uses a multidisciplinary approach to investigate two different aspects of protein biosynthesis and modification - Indirect tRNA aminoacylation pathways in Helicobacter pylori and fungal GPI membrane anchoring of proteins. We draw on techniques from biochemistry, organic and biophysical chemistry, and molecular and microbiology in order to understand these complex macromolecular processes.
GPI Membrane Anchoring of Proteins
Glycosylphosphatidylinositol (GPI) membrane anchors are complex glycolipids that are post-translationally attached to the C-termini of as many as 1% of eukaryotic proteins. Upon anchor attachment, these modified proteins are translocated to the outer cell wall where they play a variety of important cell surface functions. Our group investigates GPI transamidase (GPI-T), the enzyme that attaches GPI anchors to proteins. GPI-T is a complex enzyme, comprised of at least five subunits, all of which are membrane-bound.
We are interested in the characterization of GPI-T, both in vivo and in vitro. We are developing new tools to study this enzyme and new methodologies for its solubilization. We also seek to minimize GPI-T into a soluble enzyme that can be used to modifiy protein substrates with non-natural compounds of biophysical importance.
Indirect tRNA Aminoacylation
There are twenty proteinaceous amino acids that are commonly used by all organisms. In most cases, including humans, yeast, and E. coli, there are twenty aminoacyl-tRNA synthetases, with one enzyme responsible for attaching each encoded amino acid to the correct tRNA(s). However, in many organisms glutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase (GlnRS and AsnRS, respectively) are missing. In these cases, the corresponding aminoacyl-tRNAs, Gln-tRNAGln and Asn-tRNAAsn, are made indirectly via transamidation of Glu-tRNAGln and Asp-tRNAAsn. This biosynthetic pathway requires the presence of two misacylating AARSs and a glutamine-dependent amidotransferase (Adt).
We are investigating the indirect biosynthesis of Gln-tRNAGln and Asn-tRNAAsn in the pathogenic bacterium Helicobacter pylori. H. pylori is missing both glutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase. We are interested in understanding the evolution of direct versus indirect tRNA aminoacylation pathways as well as the mechanisms that are used by H. pylori to prevent misacylated tRNAs from entering the ribosome prior to conversion to their accurately aminoacylated counterpoints.
- B. A., Wellesley College, 1990
- Ph.D., California Institute of Technology, 1996
- NIH Postdoctoral Fellow, Massachusetts Institute of Technology, 1996-1997
- NIH Postdoctoral Fellow, The Scripps Research Institute, 1997-2000
Awards and grants
2018-2019 Drexel ELATE Fellow
2015-2016 WSU College of Liberal Arts and Sciences Excellence in Teaching Award
2011 Chair and Host, 2011 International Conference on Aminoacyl-tRNA Synthetases
2009-2010 WSU Career Development Chair Award
2007 American Cancer Society Research Scholar Award
2000 Research Corporation Innovation Award
Hendrickson, T. L. "Old enzymes versus new herbicides." 2018, J. Biol. Chem., 293, 7892-7893.
Zhao, L., Rathnayake, U. M., Dewage, S. W., Wood, W. N., Veltri, A. J., Cisneros, G. A., Hendrickson, T. L. "Characterization of tunnel mutants reveals a catalytic step in ammonia delivery by an aminoacyl-tRNA amidotransferase." 2016, Febs Lett. 590, 3122-3132.
Hendrickson, T. L. "Integrating responsible conduct of research education into undergraduate biochemistry and molecular biology laboratory curricula." 2015, Biochem. Mol. Biol. Educ., 43, 68-75.
Gamage, D. G., Hendrickson, T. L. "GPI transamidase and GPI anchored proteins: oncogenes and biomarkers for cancer." 2013, Crit. Rev. Biochem. Mol. Biol., 48, 446-464.
Silva, G. N., Fatma, S., Floyd, A. M., Fischer, F., Chuawong, P., Cruz, A. N., Simari, R. M., Joshi, N., Kern, D., Hendrickson, T. L. "A tRNA-independent mechanism for transamidsome assembly promotes aminoacyl-tRNA transamidation." 2013, J. Biol. Chem., 288, 3816-3822.
CHM 2220 Organic Chemistry II, 4 credit hours, W2019
CHM 2225 Organic Chemistry II for Engineers, 3 credit hours, W2019
CHM 2220 Organic Chemistry II, 4 credit hours, F2018
CHM 2225 Organic Chemistry II for Engineers, 3 credit hours, F2018
CHM 6635 Tools in Molecular Biology, 3 credit hours, W2018