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Article: Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3

TitleStructure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3
Authors
Issue Date2006
PublisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2006, v. 34 n. 22, p. 6621-6628 How to Cite?
AbstractHuman 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 β-barrel and a long α-helix and assumes a structure more similar to the Drosophila MOF chromo barrel domain than the typical HP1/ Pc chromo domains. The β-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 β-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. © 2006 Oxford University Press.
Persistent Identifierhttp://hdl.handle.net/10722/91889
ISSN
2015 Impact Factor: 9.202
2015 SCImago Journal Rankings: 7.458
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhang, Pen_HK
dc.contributor.authorDu, Jen_HK
dc.contributor.authorSun, Ben_HK
dc.contributor.authorDong, Xen_HK
dc.contributor.authorXu, Gen_HK
dc.contributor.authorZhou, Jen_HK
dc.contributor.authorHuang, Qen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorDing, Jen_HK
dc.date.accessioned2010-09-17T10:29:38Z-
dc.date.available2010-09-17T10:29:38Z-
dc.date.issued2006en_HK
dc.identifier.citationNucleic Acids Research, 2006, v. 34 n. 22, p. 6621-6628en_HK
dc.identifier.issn0305-1048en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91889-
dc.description.abstractHuman 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 β-barrel and a long α-helix and assumes a structure more similar to the Drosophila MOF chromo barrel domain than the typical HP1/ Pc chromo domains. The β-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 β-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. © 2006 Oxford University Press.en_HK
dc.languageengen_HK
dc.publisherOxford University Press. The Journal's web site is located at http://nar.oxfordjournals.org/en_HK
dc.relation.ispartofNucleic Acids Researchen_HK
dc.titleStructure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3en_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1093/nar/gkl989en_HK
dc.identifier.pmid17135209-
dc.identifier.pmcidPMC1747190-
dc.identifier.scopuseid_2-s2.0-33845910902en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845910902&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume34en_HK
dc.identifier.issue22en_HK
dc.identifier.spage6621en_HK
dc.identifier.epage6628en_HK
dc.identifier.isiWOS:000243191500027-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridZhang, P=7404158930en_HK
dc.identifier.scopusauthoridDu, J=8219836400en_HK
dc.identifier.scopusauthoridSun, B=15754946900en_HK
dc.identifier.scopusauthoridDong, X=15753492500en_HK
dc.identifier.scopusauthoridXu, G=7404261340en_HK
dc.identifier.scopusauthoridZhou, J=7405551483en_HK
dc.identifier.scopusauthoridHuang, Q=7403634448en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridDing, J=26643527900en_HK
dc.identifier.citeulike1008035-

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