|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.|
|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.
- Veerendra Kumar, Rya Ero, Tofayel Ahmed, Kwok Jian Goh, Yin Zhan, Shashi Bhushan, and Yong-Gui Gao. (2016). The Structure of Elongation Factor 4 (EF4/LepA) in GTP Form Bound to the Ribosome. Journal of Biological Chemistry, 291(Cover Image July), 12943-50.
- Kumar V, Chen Y, Ero R, Ahmed T, Tan J, Li Z, wong AS, Bhushan S, Gao YG. (2015). Structure of BipA in GTP form bound to the ratcheted ribosome. PNAS, 112(35), 10944-9.
- Chen Y, Feng S, Kumar V, Ero R, Gao YG. (2013). Structure of EF-G-Ribosome complex in a pretranslocation state. Nature Structural and Molecular Biology, , 2013, 20: 1077–1084 (online on 4 August 2013).
- 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).
- 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.