Nanyang Technology University

Academic Profile
Assoc Prof Gao Yonggui
Nanyang Associate Professor (NRF)
 
Division of Structural Biology & Biochemistry 
School of Biological Sciences 
College of Science 



Email: YGAO@ntu.edu.sg
Phone: (+65)63162819/65869679 
Office: Biopolis 7-04B IMCB 
Education
  • PhD Zhejiang University 2003
  • MS Zhejiang University 1997
  • BS Zhejiang University 1994
Biography
I got my Ph.D major in biochemical engineering, Zhejiang University, China, I worked as a lecturer in College of Life Science, Zhejiang University. In 2003, I moved to Professor Tanaka’s Lab funded by Center of Excellence (COE) project, Faculty of Advanced Life Science, Hokkaido University. The research topic is the structural and functional research on transcription, translational initiation control, and cellulose synthesis. Since 2008, I worked as a senior scientist in Professor Ramakrishnan Venki’s group where Nobel Prize is awarded in 2009, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK. There, I made breakthrough in understanding structure and function of ribosome with GTPase factors, for which two landmark papers were published.
Research Interests
I am interested in the field of DNA/RNA-protein interactions, particularly in the structural and functional research of translation initiation control and protein synthesis by ribosome. For the first time, I recently discovered a new crystal form from ribosome lacking the subunit L9, that allows crystallization of the ribosome in the presence of GTPase factors. Based on this, the crystal structures of the 70S ribosome with elongation factor G (EF-G) trapped by fusidic acid in the post-translocational state, and with elongation factor Tu (EF-Tu) and aminoacyl-tRNA were solved, respectively. Both structures reveal many significant aspects of ribosome functions at atomic level with regard to elongation, the heart of translation. Meanwhile, I solved crystal structures of E. coli RelE (a toxin related to riboendonucleases) bound to 70S ribosomes in the precleavage and postcleavage states, which provides a clear basis for understanding the mechanism of ribosome-dependent endonucleases (mRNA shutdown). I want to pursue further research on the structure and function of translational factors with ribosome in Singapore. I will focus on further understanding EF-G function in translation as well as in the post-termination complex with ribosome recycling factor (RRF). Meanwhile, the structural and functional protein complex associated with disease and industrial application will be targed.

Positions for Postdoc, Ph.D. Scholarship, Research Assistant or Technician are available, interested candidates are invited to email me.
Current Projects
  • Structural and functional research of macromolecules: ribosome and cellulose terminal complex
  • Structure and Functional Interactions of Translational Factors with Ribosome by X-Ray Crystallography
Selected Publications
  • Hu, S.Q.*, Gao, Y.G.*, Tajima, K.*, Sunagawa, N., Zhou, Y., Kawano, S., Yoda, T., Shimura, D., Satoh, Y., Munekata, M., Tanaka, I. and Yao, M.,. (2010). Structure of bacterial cellulose synthase subunit D octamer with four inner passageways. PNAS, 107(42), 17957-61 (*: These authors contributed equally).
  • Neubauer, C.*, Gao, Y.G.*, Andersen, K.R.*, Dunham, C., Kelley, A., Hentschel, J., Gerdes, K., Ramakrishnan, V. and Ditlev Egeskov Brodersen, D. E. (2009). The structural basis for mRNA cleavage by the ribosome-dependent endonuclease RelE. Cell, 139, 1084-1095.
  • Gao, Y.G., Maria Selmer, M., Dunham, C.M., Weixlbaumer, A., Kelley, A.C. and Ramakrishnan, V. (2009). The structure of the ribosome with elongation factor G trapped in the post-translocational state. Science, 326, 694-699.
  • Schmeing, T.M.*, Voorhees, R.M.*, Kelley, A.C., Gao, Y.G., Murphy, F.V., Weir, J.R. and Ramakrishnan, V. (2009). The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science, 326, 688-694.
  • Gao, Y.G., Suzuki, H., Itou, H., Wachi, M., Watanabe, N., Tanaka, I., and Yao, M. (2008). Structural and functional characterization of the LldR from Corynebacterium glutamicum: a transcriptional repressor involved in L-lactate and sugar utilization. Nucleic Acids Research, 36, 7110-7123.
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