Education:

B.S., Chemistry with American Chemical Society Biochemistry Certification, Purdue University

Teaching:

CHEM 010:  General Chemistry Lab

CHEM 032: Organic Chemistry II Lab

CHEM 038: Biological Chemistry I

CHEM 038: Biological Chemistry I Lab

CHEM 048: Biological Chemistry II

CHEM 108: Topics in Biochemistry

Research:

Our research group is interested in understanding the proofreading mechanisms by Aminoacyl-tRNA synthetases (aaRSs). aaRSs are universally conserved enzymes that ensure high fidelity of translation of genetic information into functional proteins across all domains of life. These enzyme pair amino acids, which are the building blocks of proteins, with their corresponding transfer RNAs (tRNAs). Once amino acids are activated and linked to corresponding tRNA by aaRSs, they are delivered to ribosome for protein synthesis. aaRSs can make error by attaching noncognate amino acid onto tRNA because the size and functional group similarity among related amino acids make it challenging for aaRSs to accurately distinguish. Incorporation of incorrect amino acids into the proteins during translation can lead to inactive or misfolded proteins which can cause diverse cellular and organismal defects ranging from cell death in microbes to neurodegeneration in mammals. Our research focuses on studying one proofreading mechanism method facilitated by free-standing trans-editing domain called ProXp-ala. In plants, ProXp-ala has a conserved C-terminal domain (CTD) of unknown origin, structure and function that is not observed in any other organisms. Our main goal is to characterize the plant-specific CTD using a variety of biochemical and structural techniques and understand the functional or structural benefits or drawbacks of CTD on plant ProXp-ala.

Recent Publication:

Byun JK, Vu JA, He SL, Jang JC, Musier-Forsyth K. Plant-exclusive domain of trans-editing enzyme ProXp-ala confers dimerization and enhanced tRNA binding. J Biol Chem. 2022 Jul 12;298(9):102255. doi: 10.1016/j.jbc.2022.102255