Song Tan

Verne M. Willaman Professor of Molecular Biology
Song Tan
Song
Tan
Verne M. Willaman Professor of Molecular Biology
Department Affiliations
Interests
Biophysics
Biochemistry
Enzymology
Gene Regulation
Structural Biology
Address
Phone
814-865-3355
Website
Tan Website

About Me

Song Tan studied physics as an undergraduate at Cornell University (1985) before pursuing his PhD at the MRC Laboratory of Molecular Biology as a Marshall Scholar (1989).  He continued his training as a postdoctoral fellow and project leader under Tim Richmond at the ETH-Zürich (Swiss Federal Institute of Technology).  Dr. Tan joined the BMB faculty in 1998 and was named a Pew Scholar in the Biomedical Sciences in 2001.  Dr. Tan’s laboratory investigates how chromatin enzymes and factors interact with their nucleosome substrates using biochemical and structural approaches. In 2020 I was appointed as holder of the Verne M. Willaman Chair in Molecular Biology.

 

Department of University Committees

  • Chair, BMB Eukaryotic Gene Regulation Faculty Search Committee
     
  • Penn State University Rhodes/Marshall/Mitchell Scholarship Selection Committee

 

Program or Departmental Affiliations

BMMB Graduate Program Molecular, Cellular, and Integrative Biosciences

 

Editorial Boards

Editorial Board, Protein Expression and Purification

 

Centers

Center for Eukaryotic Gene Regulation
Director

 

Research Summary

Gene regulation is fundamental to the proper functioning of a cell, and many cancers can be traced to abnormal gene regulation. Our goal is to understand how genes are regulated by combining genetic, biochemical and structural descriptions. Our expectation is that such information will contribute to the development of future therapeutic agents against cancer and other human diseases.

We are particularly interested in how chromatin enzymes recognize and interact with their physiological substrate, the nucleosome. Our laboratory determined the first structure of a chromatin protein/nucleosome complex (RCC1/nucleosome, 2010) and the first structure of a chromatin enzyme/nucleosome complex (PRC1/nucleosome, 2014).  These studies are just the start since there are hundreds of chromatin proteins and enzymes, many associated with human diseases. To this end, we perform biochemical studies of chromatin enzymes and nucleosomes, and we use X-ray crystallography and cryoelectron microscopy to determine their three-dimensional structures.

 

Honors or Awards

 

Selected Publications

  • Kim, S., J. Zhu, N. Yennawar, P. Eek and S. Tan (2020) Crystal structure of the LSD1/CoREST histone demethylase bound to its nucleosome substrate, Mol. Cell, 78:903-914.
     
  • Sun, J., M. Paduch, S. Kim, R.M. Kramer, A.F. Barrios, V. Lu , J. Luke, S. Usatyuk, A.A. Kossakoff and S. Tan (2018) Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2, PNAS, 115:10010-10015.
     
  • Henrici, R.C., Pecen, T.J., Johnston, J.L and Tan, S. (2017) The pPSU plasmids for generating DNA molecular weight markers, Scientific Reports, 7:2438.
     
  • McGinty, R.K., R.D. Makde and S. Tan (2016). Preparation, crystallization, and structure determination of chromatin enzyme/nucleosome complexes, Method Enzymol, 573:43-65.
     
  • Girish, T.S., R.K. McGinty and S. Tan (2016). Multivalent interactions by the Set8 histone methyltransferase with its nucleosome substrate, J. Mol Biol., 428:1531-1543.
     
  • Jennings, M.J., A.F. Barrios and S. Tan (2016). Elimination of truncated recombinant protein expressed in Escherichia coli by removing cryptic translation initiation site, Prot. Expr. Purif., 121:17-21.
     
  • McGinty, R.K. and S. Tan (2016) Recognition of the nucleosome by chromatin factors and enzymes, Curr. Opin. Struct. Biol., 21:128-136.
     
  • Kim, S., N. Chatterjee, M.J. Jennings, B. Bartholomew, and S. Tan (2015). Extranucleosomal DNA enhances the activity of the LSD1/CoREST histone demetthylase complex. Nucl. Acid Research, 43:4868-4880.
     
  • McGinty, R.K, and S. Tan (2015). Nucleosome structure and function. Chem Reviews, 115:2255-2273.
     
  • McGinty, R.K, Henrici, R.C. and S. Tan (2014). Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome. Nature, 514:591-596.
     
  • McGinty, R.K. and Tan, S. (2014). Histones, Nucleosomes, and Chromatin Structure. In Fundamentals of Chromatin, J.L. Workman and S.M. Abmayr, ed. (New York: Springer).
     
  • Makde, R.D. and Tan, S. (2013). Strategies for crystallizing a chromatin protein in complex with the nucleosome core particle. Anal. Biochem., 442:138-145.
     
  • Tan, S. and Nagai, K. (2013). Protein-nucleic Interactions, 'I have a cunning plan...'. Curr. Opin. Struct. Biol., 23:1-3
     
  • Huang, J and Tan, S. (2013). Piccolo NuA4-Catalyzed Acetylation of Nucleosomal Histones: Critical Roles of an Esa1 Tudor/Chromo Barrel Loop and an Epl1 Enhancer of Polycomb A (EPcA) Basic Region. Mol. Cell. Bio., 33:159-169.
     
  • Tan, S. (2012). Deciphering how the chromatin factor RCC1 recognizes the nucleosome: the importance of individuals in the scientific discovery process. Biochem. Soc. Trans., 40:351-356.
     
  • Chittuluru J.R., Chaban Y., Monnet-Saksouk J., Carrozza, M.J., Sapountzi, V., Selleck, W. Huang, J., Utley, R.T., Cramet, M., Allard, S., Cai, G., Workman, J.L., Fried, M.G., Tan, S., Côté, J., Asturias, F.J. (2011) Structure and nucleosome interaction of the NuA4 and Piccolo-NuA4 histone acetyltransferase complexes. Nature Mol. Str. Biol., 18, 1196-1203.
     
  • Tan, S. and Davey, C.A. (2011). Nucleosome structural studies. Curr Opin Struct Biol, 21, 128-136.
     
  • Makde, R.D., England, J.R., Yennawar, H. and Tan. S. (2010). Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature, 467:562-566.
     
  • England, J.R., Huang, J., Jennings, M.J., Makde, R.D., and Tan, S. (2010). RCC1 uses a conformationally diverse loop region to interact with the nucleosome: A model for the RCC1-nucleosome complex. J Mol Biol 398, 518-529.
     
  • Choy, J.S., Wei, S., Lee, J.Y., Tan, S., Chu, S., and Lee, T.H. (2010). DNA methylation increases nucleosome compaction and rigidity. J Am Chem Soc 132, 1782-1783.
     
  • Psathas, J.N., Zheng, S., Tan, S., and Reese, J.C. (2009). Set2-dependent K36 methylation is regulated by novel intratail interactions within H3. Mol Cell Biol 29, 6413-6426.
     
  • Selleck, W. and S. Tan (2008) Recombinant protein complex expression in E. coli, Curr Protocols Protein Sci, Chapter 5, unit 5.21.
     
  • Barrios, A., Selleck, W., Hnatkovich. B., Kramer, R., Sermwittayawong, D. and Tan, S. (2007) Expression and purification of recombinant yeast Ada2/Ada3/Gcn5 and Piccolo NuA4 histone acetyltransferase complexes, Methods, 41:271-277.
     
  • Berndsen C.E., Selleck, W., McBryant, S.J., Hansen, J.C., Tan, S. and Denu, J.M. (2007) Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex, Biochemistry, 46:2091-2099.
     
  • Berndsen, C.E., Albaugh, B.N., Tan, S. and Denu, J.M. (2007) Catalytic mechanism of a MYST family histone acetyltransferase,Biochemistry, 46:623-629. Accelerated Publication.
     
  • Sermwittayawong, D. and Tan, S. (2006) SAGA binds TBP via its Spt8 subunit in competition with DNA: implications for TBP recruitment, EMBO J, 25:3791-3800.