Scripps Research Joint Appointments

Department of Cell and Molecular Biology
Faculty, Kellogg School of Science and Technology

Research Focus

Aminoacyl-tRNA synthetases provide the algorithm of the genetic code in the first reaction of protein translation. The tRNA synthetases catalyze the attachment of amino acids to their cognate tRNAs that bear the triplet anticodon of the genetic code. While preserving their essential canonical roles in translation, aminoacyl tRNA synthetases have acquired unique functions during evolution. Human tRNA synthetases in particular have functions in diverse pathways, including angiogenesis inflammation, and apoptosis. My research group is focused on defining the novel functions of aminoacyl-tRNA synthetases in cancer etiology.

Education

B.S., Biology, University of Science and Technology of China, Hefei China , 2000
Ph.D., Structural Biology, Department of Molecular and Cell Biology, University of Science and Technology of China, Hefei China, 2005

Selected References

Guo M, Yang XL, Schimmel P. New functions of tRNA synthetases beyond translation. Nature Reviews Molecular Cell Biology, 2010 Sep;11(9):668-674.

Guo M, Chong YE, Shapiro R, Beebe K, Yang XL, Schimmel P. Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma. Nature, 2009 Dec 10; 462:808-812.

Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, Schimmel P. The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science, 2009 Aug 7; 325:744-747.

Guo M, Ignatov M, Musier-Forsyth K, Schimmel P, Yang XL. Crystal structure of tetrameric form of human lysyl-tRNA synthetase: implications for multisynthetase complex formation. Proc. Natl. Acad. Sci. USA, 2008 Feb 19;105(7):2331-2336.