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Article: UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail

TitleUHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail
Authors
Issue Date2012
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmb
Citation
Journal of Molecular Biology, 2012, v. 415 n. 2, p. 318-328 How to Cite?
AbstractHuman multi-domain-containing protein UHRF1 has recently been extensively characterized as a key epigenetic regulator for maintaining DNA methylation patterns. UHRF1 SRA domain preferentially binds to hemimethylated CpG sites, and double Tudor domain has been implicated in recognizing H3K9me3 mark, but the role of the adjacent PHD finger remains unclear. Here, we report the high-resolution crystal structure of UHRF1 PHD finger in complex with N-terminal tail of histone H3. We found that the preceding zinc-Cys4 knuckle is indispensable for the PHD finger of UHRF1 to recognize the first four unmodified residues of histone H3 N-terminal tail. Quantitative binding studies indicated that UHRF1 PHD finger (including the preceding zinc-Cys4 knuckle) acts together with the adjacent double Tudor domain to specifically recognize the H3K9me3 mark. Combinatorial recognition of H3K9me3-containing histone H3 tail by UHRF1 PHD finger and double Tudor domain may play a role in establishing and maintaining histone H3K9 methylation patterns during the cell cycle.
Persistent Identifierhttp://hdl.handle.net/10722/163769
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorXie, Sen_US
dc.contributor.authorJakoncic, Jen_US
dc.contributor.authorQian, Cen_US
dc.date.accessioned2012-09-20T07:51:28Z-
dc.date.available2012-09-20T07:51:28Z-
dc.date.issued2012en_US
dc.identifier.citationJournal of Molecular Biology, 2012, v. 415 n. 2, p. 318-328en_US
dc.identifier.issn0022-2836-
dc.identifier.urihttp://hdl.handle.net/10722/163769-
dc.description.abstractHuman multi-domain-containing protein UHRF1 has recently been extensively characterized as a key epigenetic regulator for maintaining DNA methylation patterns. UHRF1 SRA domain preferentially binds to hemimethylated CpG sites, and double Tudor domain has been implicated in recognizing H3K9me3 mark, but the role of the adjacent PHD finger remains unclear. Here, we report the high-resolution crystal structure of UHRF1 PHD finger in complex with N-terminal tail of histone H3. We found that the preceding zinc-Cys4 knuckle is indispensable for the PHD finger of UHRF1 to recognize the first four unmodified residues of histone H3 N-terminal tail. Quantitative binding studies indicated that UHRF1 PHD finger (including the preceding zinc-Cys4 knuckle) acts together with the adjacent double Tudor domain to specifically recognize the H3K9me3 mark. Combinatorial recognition of H3K9me3-containing histone H3 tail by UHRF1 PHD finger and double Tudor domain may play a role in establishing and maintaining histone H3K9 methylation patterns during the cell cycle.-
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jmben_US
dc.relation.ispartofJournal of Molecular Biologyen_US
dc.subject.meshCCAAT-Enhancer-Binding Proteins - chemistry - metabolism-
dc.subject.meshCrystallography, X-Ray-
dc.subject.meshHistones - chemistry - metabolism-
dc.subject.meshProtein Interaction Domains and Motifs-
dc.subject.meshProtein Structure, Quaternary-
dc.titleUHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tailen_US
dc.typeArticleen_US
dc.identifier.emailQian, C: cmqian@hku.hken_US
dc.identifier.authorityQian, C=rp01371en_US
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jmb.2011.11.012-
dc.identifier.pmid22100450-
dc.identifier.scopuseid_2-s2.0-84855765982-
dc.identifier.hkuros206141en_US
dc.identifier.volume415en_US
dc.identifier.issue2-
dc.identifier.spage318en_US
dc.identifier.epage328en_US
dc.identifier.isiWOS:000300032500007-
dc.publisher.placeUnited Kingdom-
dc.identifier.citeulike10030252-

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