Guo, Feng - University of California, Los Angeles - Department of Biological Chemistry

个人简介

Dr. Guo is a structural biologist and biochemist who joined the UCLA School of Medicine faculty in July 2004. He earned his B.S. in Biophysics at the Nankai University and M.S. in Physical Chemistry at the Peking University, both in China. Dr. Guo received his Ph.D. in Biochemistry and Biophysics at the University of Pennsylvania in 2000. In graduate school, he studied the Cre-loxP site-specific DNA recombination using X-ray crystallography. He was a postdoctoral fellow with Dr. Thomas Cech at the University of Colorado at Boulder, where he worked on the thermostability and crystal structure of large ribozymes.

研究领域

Structure and Function of Non-coding RNAs The functions of RNA extend far beyond coding for amino acid sequences. The Guo research group is interested in elucidating how non-coding RNAs function by forming defined three-dimensional structures and by interacting with proteins. In particular, we are investigating how the primary transcripts of microRNAs are recognized and cleaved by the Drosha nuclease and its RNA-binding partner DGCR8, and how this reaction is affected by a heme cofactor bound to the DGCR8 protein. The projects are investigated using biochemistry, structural and cell biology methods.

近期论文

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Quick-Cleveland J., Jacob J.P., Weitz S.H., Shoffner G., Senturia R., and Guo F. (2014) The DGCR8 RNA-binding heme domain recognizes primary microRNAs by clamping the hairpin. Cell Rep. 7(6):1994-2005. Link Weitz S.H., Gong M., Barr I., Weiss S., and Guo F. (2014) Processing of microRNA primary transcripts requires heme in mammalian cells. Proc. Natl. Acad. Sci. USA. 111(5):1861-6. Link Senturia, R., Laganowsky, A., Barr, I., Brooke D. Scheidemantle, B.D., and Guo, F. (2012) Dimerization and heme binding are conserved in amphibian and starfish homologues of the microRNA processing protein DGCR8. PLoS ONE 7(7): e39688. Link Gong, M., Chen, Y., Senturia, R., Ulgherait, M., Faller, M., and Guo, F. (2012) Caspases cleave and inhibit the microRNA processing protein DiGeorge Critical Region 8. Protein Sci. 21: 797-808. Link Barr I., Smith A.T., Chen Y., Senturia R., Burstyn J., Guo F. (2012) Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing. Proc. Natl. Acad. Sci. USA. 109(6):1919-1924. Link Barr I., Smith A.T., Senturia R., Chen Y., Scheidemantle B.D., Burstyn J., Guo F. (2011) DiGeorge Critical Region 8 (DGCR8) is a double-cysteine-ligated heme protein. J. Biol. Chem. 286(18):16716-25. Link Faller, M., Toso, D., Matsunaga, M., Atanasov, I., Senturia, R., Chen, Y., Zhou, Z.H., and Guo, F. DGCR8 recognizes primary transcripts of microRNAs through highly cooperative binding and formation of higher-order structures. RNA. 2010; 16: 1570-1583. Link Senturia, R., Faller, M., Yin, S., Loo, J.A., Cascio, D., Sawaya, M.R., Hwang, D., Clubb, R.T., and Guo, F. Structure of the dimerization domain of DiGeorge Critical Region 8. Protein Sci. 2010; 19: 1354-1365. Link Miallau Linda, Faller Michael, Chiang Janet, Arbing Mark, Guo Feng, Cascio Duilio, Eisenberg David Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. The Journal of Biological Chemistry. 2009; 284(1): 276-83. Link Wang Qi, Barr Ian, Guo Feng, Lee Christopher Evidence of a novel RNA secondary structure in the coding region of HIV-1 pol gene. RNA. 2008; 14(12): 2478-88. Link Faller Michael, Guo Feng MicroRNA biogenesis: there's more than one way to skin a cat. Biochimica et biophysica acta. 2008; 1779(11): 663-7. Link Faller, M., Matsunaga, M., Yin, S., Loo, J., and Guo, F. Heme is involved in microRNA processing. Nature Structural & Molecular Biology. 2007; 14(1): 23-29. Link Guo, F., Gooding, A.R. and Cech, T.R. Comparison of crystal structure interactions and thermodynamics for stabilizing mutations in the Tetrahymena ribozyme. RNA. 2006; 12: 387-395. Link Guo, F Gooding, AR Cech, TR Structure of the Tetrahymena ribozyme: base triple sandwich and metal ion at the active site. Molecular cell. 2004; 16(3): 351-62. Link