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John P. Toscano
Department Chair

JHU Department of Chemistry
137 Remsen Hall
3400 N. Charles Street
Baltimore, MD 21218

410-516-7429 phone
410-516-8420 fax
chemdept@jhu.edu email

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Tamara Hendrickson

Organic and Biochemistry

Johns Hopkins University
Remsen 124
3400 North Charles St.
Baltimore, MD 21218

Phone:  410.516.6706
Email:  hendrick@jhu.edu
Hendrickson Group Website

PhD - California Institute of Technology
NIH Post Doctoral Fellow - Massachusetts Institute of Technology and The Scripps Research Institute

The Hendrickson research group uses a multidisciplinary approach, drawing from organic and biological chemistry, genomics and molecular biology, to evaluate complex questions within the broad arena of protein biosynthesis. Research currently focuses on two distinct areas: Indirect tRNA aminoacylation reactions and glycosylphosphatidyl inositol anchoring of proteins.

Novel tRNA Aminoacylation Mechanisms
Many species thrive in the absence of specific aminoacyl-tRNA synthetases (AARSs), the highly conserved and "essential" enzymes which biosynthesize aminoacyl-tRNAs. Glutaminyl- and asparaginyl-tRNA synthetases (GlnRS and AsnRS) are the least ubiquitous AARSs. Instead, species that lack either or both of these enzymes use indirect pathways to complete their complement of aminoacylated tRNAs. These routes 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, tRNA recognition, and the evolution of the protein translation apparatus. Our lab is using a variety of approaches to address these questions, particularly from an evolutionary perspective.

Glycosylphosphatidyl inositol (GPI) Membrane Anchoring
The C-termini of GPI membrane anchored proteins are post-translationally modified to contain an extended glycolipid. As a result of this modification, GPI-anchored proteins are transported to the plasma membrane of eukaryotic cells where they are involved in a wide array of critical functions. GPI anchors are attached via the action of the GPI transamidase (GPI-T), a multi-subunit, membrane-bound enzyme localized in the plasma membrane of the endoplasmic reticulum.

Our lab is developing the first high-throughput, soluble kinetic assay for GPI-T, based on fluorescence resonance energy transfer. The development of this assay will lay the foundation for a wide array of biochemical experiments designed to characterize GPI-T and to manipulate its substrate specificity with the ultimate goal of generating new biopolymers.
 
 

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