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projects: chromatin enzymes
projects: chromaint factors

projects: DNA ladders
projects: polycistronic expression
picture & movie gallery
gallery: amino acids
gallery: secondary structure
gallery: selected proteins
gallery: protein/DNA complexes

background reading


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nucleosome core particle structure     RCC1-nucleosome crystal structure

Our cells contain chromatin factors that interact with the nucleosome to control diverse cellular processes such as DNA replication, transcription and cell division. We determined the first crystal structure of a chromatin protein bound to the nucleosome core particle in 2010. This structure shows how the RCC1 (Regulator of Chromosome Condensation) beta-propeller protein uses loops to interact with both histone and DNA components of the nucleosome. In particular, RCC1 uses an "arginine anchor" to interact with the acidic patch on the histone H2A/H2B dimer. This same interaction has been observed in all currently available crystal structures of chromatin factors in complex with the nucleosome.

Arginine anchor in chromatin factor-nucleosome complexes

Current chromatin factor projects include biochemical and structural studies of how RCC1 recruits and activates the small GTPase Ran to create the Ran-GTP gradient critical for mitosis and nucleocytoplasmic transport.

Pointers to articles in the popular press, podcasts and review articles about chromatin and chromatin modifications can be found in the background reading section.


  • McGinty, R.K., R.D. Makde and S. Tan (2016). Preparation, crystallization, and structure determination of chromatin enzyme/nucleosome compelxes, Method Enzymol, in press.

  • 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. (abstract)

  • McGinty, R.K. and S. Tan (2016) Recognition of the nucleosome by chromatin factors and enzymes, Curr. Opin. Struct. Biol., 21:128-136.

  • 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 S. Tan (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 S. Tan (2013). Strategies for crystallizing a chromatin protein in complex with the nucleosome core particle. Anal. Biochem., 442:138-145 (abstract).

  • S. Tan (2012). Deciphering how the chromatin factor RCC1 recognizes the nucleosome: the importance of individuals in the scientific discovery processs. Biochem. Soc. Trans., 40:351-356. (abstract)

  • Makde, R.D., J.R. England, H. Yennawar and S. Tan (2010). Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature, 467:562-566. (abstract)

  • England, J.R., J. Huang, M.J. Jennings, R. D. Makde, and S. Tan (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. (abstract)

video introduction | projects: | chromatin enzymes | chromatin factors | DNA ladders | polycistronic expression | picture & movie gallery: | amino acids | secondary structure | selected proteins | protein/DNA complexes |
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This page is maintained by Song Tan: (814-865-3355)
Department of Biochemistry & Molecular Biology, 108 Althouse Lab, University Park, PA 16802

This page was last updated on October 12, 2020.

Penn State BMB Eberly College of Science