Nucleic Acids Research Advance Access originally published online on November 28, 2006
Nucleic Acids Research 2006 34(22):6621-6628; doi:10.1093/nar/gkl989
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Nucleic Acids Research, 2006, Vol. 34, No. 22 6621-6628
© 2006 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Structural Biology |
Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3
1 State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences Shanghai, China 2 Graduate School of Chinese Academy of Sciences 320 Yue-Yang Road, Shanghai 200031, China 3 MacCHESS, Cornell High Energy Synchrotron Source, Cornell University Ithaca, NY 14853, USA
*To whom correspondence should be addressed. Tel: +86 21 5492 1619; Fax: +86 21 5492 1116; Email: jpding{at}sibs.ac.cn
Received August 8, 2006. Revised October 28, 2006. Accepted October 30, 2006.
Human MRG15 is a transcription factor that plays a vital role in embryonic development, cell proliferation and cellular senescence. It comprises a putative chromo domain in the N-terminal part that has been shown to participate in chromatin remodeling and transcription regulation. We report here the crystal structure of human MRG15 chromo domain at 2.2 Å resolution. The MRG15 chromo domain consists of a ß-barrel and a long 
-helix and assumes a structure more similar to the Drosophila MOF chromo barrel domain than the typical HP1/Pc chromo domains. The ß-barrel core contains a hydrophobic pocket formed by three conserved aromatic residues Tyr26, Tyr46 and Trp49 as a potential binding site for a modified residue of histone tail. However, the binding groove for the histone tail seen in the HP1/Pc chromo domains is pre-occupied by an extra ß-strand. In vitro binding assay results indicate that the MRG15 chromo domain can bind to methylated Lys36, but not methylated Lys4, Lys9 and Lys27 of histone H3. These data together suggest that the MRG15 chromo domain may function as an adaptor module which can bind to a modified histone H3 in a mode different from that of the HP1/Pc chromo domains.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors
Protein Data Bank accession code: 2F5K
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