Yeeting Esther Chong
Education
B.A. (Biology, Chemistry) Cornell University 2005
Current Research Focus
Alanyl-tRNA synthetase (AlaRS) contains an editing domain which helps maintain translational fidelity by hydrolyzing non-cognate amino acids, namely serine and glycine, that have been incorrectly charged onto tRNAAla. A mild editing defect in AlaRS has been shown to cause neurodegeneration in the mouse. A free-standing genome-encoded protein, termed AlaXp, which possesses sequence homology with the editing domain of AlaRS, has been identified across a wide range of species. This apparent redundancy of editing suggests a particular sensitivity of organisms to mistranslation at alanine positions. My research is concerned with understanding the mechanism behind the editing functions of AlaRS and AlaXp, as well as the biological role of AlaXp.
Publications
Chong YE, Yang XL, Schimmel P (2008)
“Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation.”
J Biol Chem. Oct 31;283(44):30073-8
Kim MY, Woo EM, Chong YTE, Homenko DR, Kraus WL (2006)
“Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor.”
Mol Endocrinol. Jul;20(7):1479-93.
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