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Article: Structure and chromosomal DNA binding of the SWIRM domain

TitleStructure and chromosomal DNA binding of the SWIRM domain
Authors
KeywordsSpecies Index: Moira
Issue Date2005
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nsmb/
Citation
Nature Structural And Molecular Biology, 2005, v. 12 n. 12, p. 1078-1085 How to Cite?
AbstractThe evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2α. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2α and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2α SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling. © 2005 Nature Publishing Group.
Persistent Identifierhttp://hdl.handle.net/10722/91180
ISSN
2015 Impact Factor: 13.338
2015 SCImago Journal Rankings: 12.548
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorZhang, Qen_HK
dc.contributor.authorLi, Sen_HK
dc.contributor.authorZeng, Len_HK
dc.contributor.authorWalsh, MJen_HK
dc.contributor.authorZhou, MMen_HK
dc.date.accessioned2010-09-17T10:14:18Z-
dc.date.available2010-09-17T10:14:18Z-
dc.date.issued2005en_HK
dc.identifier.citationNature Structural And Molecular Biology, 2005, v. 12 n. 12, p. 1078-1085en_HK
dc.identifier.issn1545-9993en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91180-
dc.description.abstractThe evolutionarily conserved Swi3p, Rsc8p and Moira (SWIRM) domain is found in many chromosomal proteins involved in chromatin modifications or remodeling. Here we report the three-dimensional solution structure of the SWIRM domain from the human transcriptional adaptor ADA2α. The structure reveals a five-helix bundle consisting of two helix-turn-helix motifs connected by a central long helix, reminiscent of the histone fold. Using structural and biochemical analyses, we showed that the SWIRM domains of human ADA2α and SMARC2 bind to double-stranded and nucleosomal DNA, and we identified amino acid residues required for this function. We demonstrated that the ADA2α SWIRM domain is colocalized with lysine-acetylated histone H3 in the cell nucleus and that it potentiates the ACF remodeling activity by enhancing accessibility of nucleosomal linker DNA bound to histone H1. These data suggest a functional role of the SWIRM domain in chromatin remodeling. © 2005 Nature Publishing Group.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/nsmb/en_HK
dc.relation.ispartofNature Structural and Molecular Biologyen_HK
dc.subjectSpecies Index: Moiraen_HK
dc.subject.meshAdaptor Proteins, Signal Transducing - analysis - chemistry - metabolismen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshCell Nucleus - chemistryen_HK
dc.subject.meshChromatin - metabolismen_HK
dc.subject.meshChromatin Assembly and Disassemblyen_HK
dc.subject.meshChromosomes - metabolismen_HK
dc.subject.meshDNA - metabolismen_HK
dc.subject.meshHelix-Turn-Helix Motifsen_HK
dc.subject.meshHistones - analysis - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshNucleosomes - metabolismen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshTranscription Factors - analysis - chemistry - metabolismen_HK
dc.titleStructure and chromosomal DNA binding of the SWIRM domainen_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.doi10.1038/nsmb1022en_HK
dc.identifier.pmid16299514-
dc.identifier.scopuseid_2-s2.0-28544433624en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-28544433624&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume12en_HK
dc.identifier.issue12en_HK
dc.identifier.spage1078en_HK
dc.identifier.epage1085en_HK
dc.identifier.eissn1545-9985-
dc.identifier.isiWOS:000233774300017-
dc.publisher.placeUnited Statesen_HK
dc.identifier.f10001029468-
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridZhang, Q=35546936300en_HK
dc.identifier.scopusauthoridLi, S=8653167300en_HK
dc.identifier.scopusauthoridZeng, L=7401904457en_HK
dc.identifier.scopusauthoridWalsh, MJ=7402337089en_HK
dc.identifier.scopusauthoridZhou, MM=7403506618en_HK
dc.identifier.citeulike420382-

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