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Chromatin Biology and Epigenetics

Group Site: 
toronto
Group Leader: 

Jinrong Min, Ph.D.

Group Info

Research Areas

The Chromatin Biology and Epigenetics Group at the Structural Genomics Consortium (SGC), University of Toronto, aims to characterize chromatin proteins by X-ray crystallography in combination with other biochemical and biophysical techniques. Research in the chromatin structual biology group consists of

1) Chromain modifying enzymes: chromatin structure is very dynamics, and the dynamic chromatin structure is governed by different chromatin modifying activities, such as DNA modification, histone modification and ATP-dependent chromatin remodeling. My laboratory is trying to understand the mechanisms of catalysis and inhibition of these chromatin modifying enzymes.

2) Regulation and recruitment of chromatin modifying activities:  Regulation and recruitment of chromatin-modifying activities is critical for establishing and maintaining normal gene expression patterns, and aberrant gene expression is linked to many human diseases, such as various genetic diseases and cancers. Chromatin-modifying activities have been relatively well characterized, but the regulation and recruitment mechanisms of chromatin-modifying activities are poorly understood. One major focus of my laboratory is to identify and characterize the recruitment and regulation mechanisms of the chromatin modifying activities.

Group Members
Chao Xu, Postdoctoral fellow

Chao received his PhD degree from the School of Life Sciences, University of Sciences and Technology of China in 2005. He joined the SGC in 2009 after conducting post-doctoral research at Mayo Clinic College of Medicine.

Chuanbing Bian, Postdoctoral fellow

Chuanbing completed his Ph.D. at the Fujian Institute of Research  on the Structure of Matter, Chinese Academy of Science.  He joined the SGC in 2009 as a post-doctoral fellow. Chuanbing is currently working on chromatin proteins involved in regulation and targeting of chromatin modifying activies.

Vinod Nayak, Postdoctoral fellow

Vinod Nayak received his PhD from the University of Pennsylvania in 2006. He joined the SGC in April 2011 after conducting post-doctoral research at Yale University and Scripps Florida.

Ke Liu, PhD student

 Ke obtained a Masters degree from the Huazhong Normal University in 2009, and currenly is a PHD student, focusing on structural and functional studies of Tudor domain proteins.

Structures

Selected  structures.  (RCSB for all the structures)

1.  Crystal structure of SGF29 in complex with H3K4me3 peptide

   

Bian C, Xu C, Ruan J, Lee KK, Burke TL, Tempel W, Barsyte D, Li J, Wu M, Zhou BO, Fleharty BE, Paulson A, Allali-Hassani A, Zhou JQ, Mer G, Grant PA, Workman JL, Zang J, Min J  (2011) Sgf29 Binds Histone H3K4me2/3 and Is Required For SAGA Complex Recruitment and Histone H3 Acetylation. EMBO J 30(14):2829-42

2. CFP1 CXXC domain in complex with a nonmethylated CpG DNA

Xu C, Bian C, Lam R, Dong A, Min J (2011) The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain. Nature Communications 2:227.

3.  Crystal structure of mature apo-Cathepsin L C25A mutant in complex with Gln-Leu-Ala peptide

Adams-Cioaba MA, Krupa JC, Xu C, Mort JS, Min J (2011) Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nature Communications 2:197.

4. Human embryonic ectoderm development (EED) in complex with a trimethylated H3K27 peptide

Xu C, Bian C, Yang W, Galka M, Ouyang H, Chen C, Qiu W, Liu H, Jones AE, Mackenzie F, Pan P, Li SS, Wang H, Min J (2010) Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proc Natl Acad Sci U S A. 107(45):19266-71.

5. Structure of human SND1 extended tudor domain in complex with the symmetrically dimethylated arginine PIWIL1 peptide R4me2s

Liu K, Chen C, Guo Y, Lam R, Bian C, Xu C, Zhao DY, Jin J, MacKenzie F, Pawson T, Min J (2010) Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proc Natl Acad Sci U S A. 107(43):18398-403.

6. Crystal structure of L3MBTL1 in complex with H4K20Me2

Min, J., Allali-Hassani, A., Nady, N., Qi, C., Ouyang,H., Liu, Y.S., MacKenzie, F., Vedadi, M. and Arrowsmith, C.H. (2007) L3MBTL1 recognition of mono- and dimethylated histones. Nat Struct Mol Biol. 14(12):1229-30


7. Crystal structure of WDR5 in complex with trimethylated H3K4 peptide

Schuetz, A, Allali-Hassani, A., Martin, F., Loppnau, P., Vedadi, M., Bochkarev, A., Plotnikov, A.N., Arrowsmith, C.H., and Min, J (2006) Structural basis for molecular recognition and presentation of histone H3 by WDR5. EMBO J. 25, 4245-4252

Publications

Selected Publications (PUBMED for all publications)

Bian C, Xu C, Ruan J, Lee KK, Burke TL, Tempel W, Barsyte D, Li J, Wu M, Zhou BO, Fleharty BE, Paulson A, Allali-Hassani A, Zhou JQ, Mer G, Grant PA, Workman JL, Zang J, Min J  (2011) Sgf29 Binds Histone H3K4me2/3 and Is Required For SAGA Complex Recruitment and Histone H3 Acetylation. EMBO J 30(14):2829-42

Nayak V, Xu C and Min J (2011) Composition, Recruitment and Regulation Of the PRC2 Complex. Nucleus 2:4, 277-282

Xu C, Bian C, Lam R, Dong A, Min J (2011) The structural basis for selective binding of non-methylated CpG islands by the CFP1 CXXC domain. Nature Communications 2:227.

Adams-Cioaba MA, Krupa JC, Xu C, Mort JS, Min J (2011) Structural basis for the recognition and cleavage of histone H3 by cathepsin L. Nature Communications 2:197.

Xu C, Bian C, Yang W, Galka M, Ouyang H, Chen C, Qiu W, Liu H, Jones AE, Mackenzie F, Pan P, Li SS, Wang H, Min J (2010) Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2). Proc Natl Acad Sci U S A. 107(45):19266-71.

Liu K, Chen C, Guo Y, Lam R, Bian C, Xu C, Zhao DY, Jin J, MacKenzie F, Pawson T, Min J (2010) Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proc Natl Acad Sci U S A. 107(43):18398-403.

Chen C, Jin J, James DA, Adams-Cioaba MA, Park JG, Guo Y, Tenaglia E, Xu C, Gish G, Min J, Pawson T. (2009) Mouse Piwi interactome identifies binding mechanism of Tdrkh Tudor domain to arginine methylated Miwi. Proc Natl Acad Sci U S A. 106(48):20336-41.

Min, J., Allali-Hassani, A., Nady, N., Qi, C., Ouyang,H., Liu, Y.S., MacKenzie, F., Vedadi, M. and Arrowsmith, C.H. (2007) L3MBTL1 recognition of mono- and dimethylated histones. Nat Struct Mol Biol. 14(12):1229-30

Schuetz, A, Allali-Hassani, A., Martin, F., Loppnau, P., Vedadi, M., Bochkarev, A., Plotnikov, A.N., Arrowsmith, C.H., and Min, J (2006) Structural basis for molecular recognition and presentation of histone H3 by WDR5. EMBO J. 25, 4245-4252

Contact

Jinrong Min, PhD
Principal Investigator, Chromatin Structural Biology
Structural Genomics Consortium
Assistant Professor, Department of Physiology
University of Toronto
101 College St., Toronto
On M5G 1L7, Canada
Tel: 416-9463868
Email:  jr [dot] min[at]utoronto [dot] ca

Mailing address:

Jinrong Min
Structural Genomics Consortium
University of Toronto
MaRS Centre, South Tower
101 College St., Rm 736
Toronto, ON, M5G 1L7
Canada

Alumni

                           

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