课题组网站： http://www.scripps.edu/guo/

Scripps Research Joint Appointments

Department of Cell and Molecular Biology
Faculty, Graduate Program

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

2010-2014

Kim DG, Lee JY, Kwon NH, Fang P, Zhang Q, Wang J, Young NL, Guo M, Cho HY, Mushtaq AU, Jeon YH, Choi JW, Han JM, Kang HW, Joo JE, Hur Y, Kang W, Yang H, Nam DH, Lee MS, Lee JW, Kim ES, Moon A, Kim K, Kim D, Kang EJ, Moon Y, Rhee KH, Han BW, Yang JS, Han G, Yang WS, Lee C, Wang MW, Kim S. Chemical inhibition of prometastatic lysyl-tRNA synthetase-laminin receptor interaction. Nature Chemical Biology,  2014 Jan;10(1):29-34.

Guo M, Schimmel P. Essential nontranslational functions of tRNA synthetases. Nature Chemical Biology, 2013 Mar; 9(3):145-53.

Ofir-Birin Y, Fang P, Bennett SP, Zhang HM, Wang J, Rachmin I, Shapiro R, Song J, Dagan A, Kim S, Marshall AG, Schimmel P, Yang XL, Nechushtan H, Razin E, Guo M. Structural switch of lysyl-tRNA synthetase function between translation and transcription. Mol. Cell, 2013. Jan 10; 49(1):30-42.

Wang J, Fang P, Schimmel P, Guo M.  Side Chain Independent Recognition of Aminoacyl-Adenylates by the Hint1 Transcription Suppressor. Journal of Physical Chemistry, 2012 Jun 14; 116(23):6798-805

Guo M, Schimmel P. Structural analyses clarify the complex control of mistranslation by tRNA synthetases. Curr. Opin. Struct. Biology, 2012 Feb; 22(1):119-26.

Xu XL, Shi Y, Zhang HM, Marshall AG, Guo M, Kishi S, Yang XL. Unique domain appended to vertebrate tRNA synthetase is essential for vascular development. Nature Communications, 2012 Feb 21; 3:681

He W, Zhang HM, Chong YE, Guo M, Marshall AG, Yang XL. Dispersed disease-causing neomorphic mutations on a single protein promote the same localized conformational opening. Proc. Natl. Acad. Sci. USA, 2011 Jul 26; 108(30):12307-12

Fang P, Zhang HM, Shapiro R, Marshall AG, Schimmel P, Yang XL, Guo M. Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex. Proc. Natl. Acad. Sci. USA, 2011 May 17; 108(20):8239-44

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

Prior to 2010

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.

Guo M, Xu F, Yamada J, Egelhofer T, Gao Y, Hartzog GA, Teng M, Niu L. Core structure of the yeast Spt4-Spt5 Complex: a conserved module for regulation of transcription elongation. Structure, 2008 Nov 12; 16:1649-1658