[ Research Interests ] [ Representative Publications ]

Tamara Hendrickson Assistant Professor Department of Chemistry Assistant Professor Department of Biology B.A. Wellesley College Ph.D. California Institute of Technology

Department of Chemistry Johns Hopkins University 3400 North Charles Street Baltimore, MD 21218-2685 U.S.A. Office Telephone: Lab Telephone: Department Fax: Email 410.516.6706 410.516.8906   hendrick@jhu.edu   Remsen Hall 122

Research Interests The Hendrickson research group uses a multidisciplinary approach, drawing from organic and biophysical chemistry, biochemistry, genomics and molecular biology, to evaluate complex questions within the broad arena of protein biosynthesis. Research currently focuses on novel and unexpected aspects of tRNA aminoacylation in pathogenic bacteria and in organisms that thrive at extreme temperatures (~70-100 °C). The recent wealth of available genome sequences from a variety of different organisms has demonstrated that many species thrive in the absence of specific aminoacyl-tRNA synthetases (AARSs), the highly conserved and "essential" enzymes that biosynthesize aminoacyl-tRNA. The most common examples are organisms that lack glutaminyl- and/or asparaginyl-tRNA synthetase (GlnRS and AsnRS). These species use indirect pathways to tRNA aminoacylation that rely on other AARSs, tRNA misacylation, and subsequent repair to generate the correct aminoacyl-tRNAs. These unexpected mechanisms of tRNA aminoacylation raise a number of intriguing questions about protein biosynthesis and the evolution of the protein translation apparatus. Some specific projects in the Hendrickson lab include: the characterization of unique patterns in tRNA-protein recognition; a mechanistic examination of novel enzymes and proteins in pathogenic bacteria and in extreme life forms; and the use of organic chemical reactivity to explain the delayed appearance of specific AARSs during evolution. Representative Publications Chuawong, P.; Hendrickson, T. L. (2006). The non-discriminating aspartyl-tRNA synthetase from Helicobacter pylori: Anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity. Biochemistry 45, 8079-8087. Stanley, A. M.; Chuawong, P.; Hendrickson, T. L.; Fleming, K. G. (2006). Energetics of outer Membrane Phospholipase A (OMPLA) Dimerization. J. Mol. Biol. 358, 120-131. Cathopoulis, T.; Chuawong, P.; Hendrickson, T. L. (2006). A Thin-Layer Electrophoretic Assay for Asp-tRNAAsn/Glu-tRNAGln Amidotransferase. Anal. Biochem., in press. Stanley, A. M.; Chuawong, P.; Hendrickson, T. L.; Fleming, K. G. (2006). Energetics of outer Membrane Phospholipase A (OMPLA) Lipid Chain Selectivity. J. Mol. Biol., in press. Hendrickson, T.L., T.K. Nomanbhoy, V. de Crecy-Lagard, and P. Schimmel. (2001). Mutational separation of two pathways for editing by a Class I tRNA synthetase. Cell 9:353-362. Doring, V., H. Mootz, L.A. Nagle, T.L. Hendrickson, V. de Crecy-Lagard, P. Schimmel, and P. Marliere. (2001). Englarging the Amino Acid Set of Escherichia coli by Infiltration of the Valine-coding Pathway. Science 292:501-504.   Hendrickson, T.L., T.K. Nomanbhoy, and P. Schimmel. (2000). Errors from selective disruption of the editing center in a tRNA synthetase. Biochemistry 39:8180. Nomanbhoy, T.K., T.L. Hendrickson, and P. Schimmel (1999). Transfer RNA-dependent translocation of misactivated amino acids to prevent errors in protein synthesis. Mol. Cell 4:519-528. Nureki, O., D.G. Vassylyev, M. Tateno, A. Shimada, T. Nakama, S. Fukai, M. Konno, T.L. Hendrickson, P. Schimmel, and S. Yokoyama (1998). Enzyme structure with two catalytic sites for double-sieve selection of substrate. Science 280:578-582. Hendrickson, T.L., J.R. Spencer, M. Kato, and B. Imperiali (1996). Design and evaluation of potent inhibitors of asparagine-linked protein glycosylation. J. Am. Chem. Soc. 118:7636-7637. Hendrickson, T.L., and B. Imperiali (1995). Metal ion dependence of oligosaccharyl transferase: Implications for catalysis. Biochemistry 34:9444-9450.

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