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Article: Structure and hemimethylated CpG binding of the SRA domain from human UHRF1

TitleStructure and hemimethylated CpG binding of the SRA domain from human UHRF1
Authors
Qian, CLi, SJakoncic, JZeng, LWalsh, MJZhou, MM
KeywordsSpecies Index: Mammalia
Issue Date2008
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2008, v. 283 n. 50, p. 34490-34494 How to Cite?
DOI: http://dx.doi.org/10.1074/jbc.C800169200
AbstractHuman UHRF1(ubiquitin-like PHD and RING finger 1) functions to maintain CpG DNA methylation patterns through DNA replication by co-localizing with the DNA methyltransferase DNMT1 at chromatin in mammals. Recent studies show that UHRF1 binds selectively to hemimethylated CpG via its conserved SRA (SET- and RING finger-associated) domain. However, the underlying molecular mechanism is not known. Here, we report a 1.95 Å resolution crystal structure of the SRA domain of human UHRF1. Using NMR structure-guided mutagenesis, electrophoretic mobility shift assay, and fluorescence anisotropy analysis, we determined key amino acid residues for methyl-DNA binding that are conserved in the SRA domain.
Persistent Identifierhttp://hdl.handle.net/10722/91181
ISSN
0021-9258
2020 Impact Factor: 5.157
2020 SCImago Journal Rankings: 2.361
PubMed Central ID
PMC2596396
ISI Accession Number ID
WOS:000261469100002
Funding AgencyGrant Number
NMR
Brookhaven National LaboratoryX4C
X6A
National Institutes of HealthGM073207
Funding Information:

The work was supported, in whole or in part, by National Institutes of Health, Grant GM073207 (to M.-M.Z.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. Section 1734 solely to indicate this fact. We acknowledge the use of the NMR facilities at the New York Structural Biology Center and thank the staff at the Brookhaven National Laboratory (beamlines X4C and X6A) for facilitating x-ray data collection. We also thank A. Plotnikov and G. Chai for helpful discussion.

References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorLi, Sen_HK
dc.contributor.authorJakoncic, Jen_HK
dc.contributor.authorZeng, Len_HK
dc.contributor.authorWalsh, MJen_HK
dc.contributor.authorZhou, MMen_HK
dc.date.accessioned2010-09-17T10:14:20Z-
dc.date.available2010-09-17T10:14:20Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2008, v. 283 n. 50, p. 34490-34494en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91181-
dc.description.abstractHuman UHRF1(ubiquitin-like PHD and RING finger 1) functions to maintain CpG DNA methylation patterns through DNA replication by co-localizing with the DNA methyltransferase DNMT1 at chromatin in mammals. Recent studies show that UHRF1 binds selectively to hemimethylated CpG via its conserved SRA (SET- and RING finger-associated) domain. However, the underlying molecular mechanism is not known. Here, we report a 1.95 Å resolution crystal structure of the SRA domain of human UHRF1. Using NMR structure-guided mutagenesis, electrophoretic mobility shift assay, and fluorescence anisotropy analysis, we determined key amino acid residues for methyl-DNA binding that are conserved in the SRA domain.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.subjectSpecies Index: Mammaliaen_HK
dc.titleStructure and hemimethylated CpG binding of the SRA domain from human UHRF1en_HK
dc.typeArticleen_HK
dc.identifier.emailQian, C:cmqian@hku.hken_HK
dc.identifier.authorityQian, C=rp01371en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.C800169200en_HK
dc.identifier.pmid18945682-
dc.identifier.pmcidPMC2596396-
dc.identifier.scopuseid_2-s2.0-58049193603en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-58049193603&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume283en_HK
dc.identifier.issue50en_HK
dc.identifier.spage34490en_HK
dc.identifier.epage34494en_HK
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000261469100002-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridLi, S=8653167300en_HK
dc.identifier.scopusauthoridJakoncic, J=12242396300en_HK
dc.identifier.scopusauthoridZeng, L=7401904457en_HK
dc.identifier.scopusauthoridWalsh, MJ=7402337089en_HK
dc.identifier.scopusauthoridZhou, MM=7403506618en_HK
dc.identifier.issnl0021-9258-

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