Tamara Lynn Hendrickson (dy8142)

University information

Title: Professor
Unit: Chemistry
Department: College of Liberal Arts & Science

Contact information

313-577-6914
Chemistry - 169
Chemistry
Liberal Arts and Sciences
Detroit, 48201

College of Liberal Arts and Sciences

Department:

Chemistry

Title: Professor
Phone: 313-577-6914
Fax: 313-577-8822
Office:

Chem 365

Social Media: https://twitter.com/Prof_Tamara
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 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 – Degrees, Licenses, Certifications: 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.

Tamara Lynn Hendrickson

Office of Diversity, Equity and Inclusion

Title: College of Liberal Arts and Sciences (CLAS), Chemistry, Professor
Tamara Lynn Hendrickson

Courses taught by Tamara Lynn Hendrickson

Fall Term 2024 (future)

Fall Term 2023

Winter Term 2023

Fall Term 2022

Winter Term 2022

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