Tamara Hendrickson

Tamara Hendrickson

Department

Chemistry

Research interest(s)/area of expertise

Indirect tRNA aminoacylation, accuracy mechanisms in protein biosynthesis, membrane proteins, protein-protein interactions, enzyme kinetics, diversity in STEM, women in STEM

Research

Our research group uses a multidisciplinary approach to investigate indirect tRNA aminoacylation pathways in pathogenic bacteria. We draw on techniques from biochemistry, biophysical chemistry, and molecular and microbiology in order to understand these complex macromolecular processes.

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  pathogenic bacteria, including H. pylori and S. aureus 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.

Education

• 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

Selected publications

Ness, Travis J.; Gamage, D.G.; Ekayanaka, S.A.; Hendrickson, T.L. "A soluble, minimalistic glycosylphosphatidylinositol transamidase (GPI-T) retains transamidation activity." 2022, Biochemistry, 61, 1273-1285. DOI: 10.1021/acs.biochem.2c00196.

Humphreys, I. R.; Pei, J.; Baek, M.; Krishnakumar, A.; Anishchenko, I.; Ovchinnikov, S.; Zhang, J.; Ness, T. J.; Banjade, S.; Bagde, S. R.; Stancheva, V. G.; Li, X.-H.; Liu, K.; Zheng, Z.; Barrero, D. J.; Roy, U.; Kuper, J.; Fernández, I. S.; Szakal, B.; Branzei, D.; Rizo, J.; Kisker, C.; Greene, E. C.; Biggins, S.; Keeney, S. Miller, E. A.; Fromme, C. J.; Hendrickson, T. L.; Cong, Q.; Baker, D. “Computed structures of core eukaryotic protein complexes.” 2021, Science, 10, eabm4805. DOI: 10.1126/science.abm4805.

Li, Y.-Y.; Cai, R.-J.; Yang, J.-Y.; Hendrickson, T. L.; Xiang, Y.; Javid, B. “Clinically relevant mutations of mycobacterial GatCAB inform regulation of translational fidelity.” 2021, mBIO, 12, e0110021. DOI: 10.1128/mBio.01100-21.

Hendrickson, T. L.; Wood, W. N.; Rathnayake, U. “Did amino acid side chain reactivity dictate the timing of aminoacyl-tRNA synthetase and protein code evolution?” 2021, 12, 409. DOI: 10.3390/genes12030409 (https://www.mdpi.com/2073-4425/12/3/409).

Rathnayake, U. M.; Hendrickson, T. L. “Bacterial aspartyl-tRNA synthetases have moderate glutamyl-tRNA synthetase activity.” 2019, Genes, 10, E262. doi: 10.3390/genes10040262.

Gamage, D. G.; Varma, Y.; Meitzler, J. L.; Morissette, R.; Ness, T. J., Hendrickson, T. L. “The soluble domains of Gpi8 and Gaa1, two subunits of glycosylphosphatidylinositol transamidase (GPI-T), assemble into a complex.” 2017, Arch. Biochem. Biophys. 633, 58-67.
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.

Courses taught by Tamara Hendrickson

Winter Term 2023 (current)

• CHM5600 - Survey of Biochemistry
• CHM7600 - Structure and Function of Biomolecules

Fall Term 2022

• CHM6270 - Advanced Bioorganic Chemistry and Drug Design
• CHM6620 - Metabolism: Pathways and Regulation
• CHM7270 - Advanced Bioorganic Chemistry and Drug Design
• CHM7620 - Metabolism: Pathways and Regulation

Winter Term 2022

• CHM5600 - Survey of Biochemistry
• CHM7600 - Structure and Function of Biomolecules
• PHC8888 - Survey of Research at the Chemistry Biology Interface

Fall Term 2021

• CHM6620 - Metabolism: Pathways and Regulation
• CHM6740 - Laboratory Safety
• CHM7620 - Metabolism: Pathways and Regulation