Haiwei SONG

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	Haiwei SONG
	Lab Location: #7-14 email: haiwei@imcb.a-star.edu.sg tel:65869700
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	Key Publications
	Chen L, Muhlrad D, Hauryliuk V, Cheng Z, Lim MK, Shyp V, Parker R and Song H (2010) Structure of the Dom34-Hbs1 Complex and implications for No-Go decay. Nat. Struct. & Mol. Biol. 17, 1233-40. Chen L, Chan SW, Zhang X, Walsh M, Lim CJ, Hong W and Song H (2010) Structural basis of YAP recognition by TEAD4 in the Hippo pathway Genes & Development, 24, 290-300. Cheng Z, Saito K, Pisarev AV, Wada M, Pisareva VP, Pestova TV, Gajda M, Round A, Kong C, Lim M, Nakamura Y, Svergun DI, Ito K, Song H. (2009). Structural insights into eRF3 and stop codon recognition by eRF1. Genes & Development 23, 1106-1118. She, M, Decker CJ, Svergun DI, Round A, Chen N, Muhlrad D, Parker R, Song H (2008). Structural basis of Dcp2 recognition and activation by Dcp1. Mol. Cell 29, 337-349. Gao, H., Zhou, Z., Rawat, U., Huang, C., Bouakaz, L., Wang, C., Cheng, Z., Liu, Y., Zavialov, A., Gursky, R., Sanyal, S., Ehrenberg, M., Frank, J. and Song H. (2007). RF3 Induces ribosomal conformational changes responsible for the dissociation of class-I release factor. Cell 129, 929-941. Cheng, Z., Muhlrad, D., Lim, M. K., Parker R. and Song H. (2007). Structural and functional insights into the human Upf1 helicase core. EMBO J. 26, 253-264. She, M., Decker C.J., Chen, N., Tumati S., Parker R. and Song H (2006). Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat. Struct. & Mol. Biol. 13, 63-70. She, M., Decker, C.J., Sundramurthy, K., Liu, Y., Chen, N., Parker, R., and Song, H. (2004). Crystal structure of Dcp1p and its functional implications in mRNA decapping. Nat. Struct. & Mol. Biol. 11, 249-56. Kong, C.G., Ito, K., Walsh, A. M., Wada, M., Liu, Y.Y., 4Kumar, S., Barford, D., Nakamura,Y. and Song, H. (2004). Crystal Structure and Functional Analysis of the Eukaryotic Class II Release Factor eRF3 from S. pombe. Mol. Cell 14, 233-245. Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D. (2000) The Crystal Structure of Human Eukaryotic Release Factor eRF1-Mechanism of Stop Codon Recognition and Peptidyl-tRNA Hydrolysis. Cell, 100, 311-321.
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		Haiwei SONG
		Haiwei SONG received his BSc (1987) in Chemistry from Henan University, MSc (1990) in Molecular Biology from the Institute of Biophysics, China and PhD (1998) in Molecular Biology in Leeds University, UK. He worked as a Postdoctoral Research Associate in the Laboratory of Molecular Biophysics in Oxford University and Institute of Cancer Research in London before he joined the former Institute of Molecular Agrobiology as a Principal Investigator in 2001. He joined IMCB in 2002 and is currently a Research Director/Professor.

		Translation Termination and Messenger RNA Decay
		Dr. Song’s research focuses on two closely related areas: the mechanism of translation termination in protein biosynthesis and the mechanism of eukaryotic mRNA decay Translation Termination The process of translation termination is mediated by polypeptide release factors (RFs) and GTP. In prokaryotes, two similar proteins, RF1 and RF2, function as class I release factors, whereas a structurally unrelated protein, RF3, is identified as the class II release factor. In eukaryotes, eRF1 (class I) functions as an omnipotent release factor; eRF3 (class II) is a GTPase and essential for cell growth and forms a stable complex with eRF1. Structural studies on individual release factor and eRF1/eRF3 complex will provide vital information on the molecular mechanism of translation termination. Sup35 (eRF3 in yeast) not only play an important role in yeast translation termination process but also share many of the characteristics of prion proteins responsible for the mammalian prion diseases including BSE and human CJD. The protein undergoes a conformational change from a soluble form to an aggregated fibre-like form in auto- catalytic process. Structure studies of Sup35 protein in both soluble and aggregated fibre-like forms will provide information concerning this process and also on the related processed associated with the mammalian prions. mRNA decay Correct regulation of gene expression is essential for the homeostasis of an organism, playing a pivotal role in cellular proliferation, differentiation, and response to specific stimuli. Modulation of mRNA stability plays an important role in regulating gene expression and dysregulation of mRNA stability has been associated with human diseases including cancer, inflammatory disease, and Alzheimer's disease. Eukaryotic mRNAs are protected at their 5' and 3' ends by the cap and poly(A) tail. The rate limiting step in decay of most mRNAs is the removal of these elements. In eukaryotes, two general pathways of mRNA decay have been identified. Both pathways are initiated with deadenylation of the 3'-poly(A) tail of mRNAs. In the 5’ to 3’ decay pathways, the 5’ cap structure can be removed by the Dcp1p/Dcp2p complex following deadenylation, thus exposing the 5’ end to 5’-3’ exoribonuclease activities. In the 3’-5’ decay pathways, deadenylation is followed by exosome-dependent 3’-5’ degradation of mRNA body. In addition, a specialized mRNA decay pathway termed nonsense-mediated mRNA decay (NMD) recognizes and degrades aberrant mRNAs that have acquired premature translation termination codons due to failure in mRNA processing or to genetic mutation. There are around 200 human genetic diseases that result from the premature translation termination. Studies of the proteins required for NMD may lead to rational approaches for the treatment of these genetic disorders. Our lab uses X-ray crystallography in conjunction with biochemical, biophysical and molecular biology methods to elucidate structure and function of the proteins and complexes involved in the mRNA decay pathways.