Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/32352
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dc.contributor.authorMillard, Christopher J.-
dc.contributor.authorWatson, Peter J.-
dc.contributor.authorCelardo, Ivana-
dc.contributor.authorGordiyenko, Y.-
dc.contributor.authorCowley, Shaun M.-
dc.contributor.authorRobinson, C. V.-
dc.contributor.authorFairall, Louise-
dc.contributor.authorSchwabe, John W. R.-
dc.date.accessioned2015-06-04T13:26:11Z-
dc.date.available2015-06-04T13:26:11Z-
dc.date.issued2013-06-20-
dc.identifier.citationMolecular Cell, 2013, 51 (1), pp. 57-67en
dc.identifier.issn1097-2765-
dc.identifier.urihttp://www.sciencedirect.com/science/article/pii/S1097276513004073en
dc.identifier.urihttp://hdl.handle.net/2381/32352-
dc.descriptionPMCID: PMC3710971 The coordinates and structure factors for the HDAC1:MTA1 complex crystal structure reported in this paper have been deposited in the Protein Data Bank under accession code 4bkx.en
dc.description.abstractClass I histone deacetylases (HDAC1, HDAC2, and HDAC3) are recruited by cognate corepressor proteins into specific transcriptional repression complexes that target HDAC activity to chromatin resulting in chromatin condensation and transcriptional silencing. We previously reported the structure of HDAC3 in complex with the SMRT corepressor. This structure revealed the presence of inositol-tetraphosphate [Ins(1,4,5,6)P4] at the interface of the two proteins. It was previously unclear whether the role of Ins(1,4,5,6)P4 is to act as a structural cofactor or a regulator of HDAC3 activity. Here we report the structure of HDAC1 in complex with MTA1 from the NuRD complex. The ELM2-SANT domains from MTA1 wrap completely around HDAC1 occupying both sides of the active site such that the adjacent BAH domain is ideally positioned to recruit nucleosomes to the active site of the enzyme. Functional assays of both the HDAC1 and HDAC3 complexes reveal that Ins(1,4,5,6)P4 is a bona fide conserved regulator of class I HDAC complexes.en
dc.description.sponsorshipThis work was supported by grant WT085408 from the Wellcome Trust.en
dc.language.isoenen
dc.publisherElsevier (Cell Press)-
dc.relation.urihttp://www.ncbi.nlm.nih.gov/pubmed/23791785-
dc.rightsOpen access under CC BY-NC-ND license. https://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.subjectAmino Acid Sequenceen
dc.subjectDimerizationen
dc.subjectHEK293 Cellsen
dc.subjectHistone Deacetylase 1en
dc.subjectHistone Deacetylasesen
dc.subjectHumansen
dc.subjectInositol Phosphatesen
dc.subjectModels, Molecularen
dc.subjectMolecular Sequence Dataen
dc.subjectProtein Foldingen
dc.subjectProtein Structure, Tertiaryen
dc.subjectRepressor Proteinsen
dc.subjectSubstrate Specificityen
dc.titleClass I HDACs share a common mechanism of regulation by inositol phosphates.en
dc.typeJournal Articleen
dc.identifier.doi10.1016/j.molcel.2013.05.020-
dc.identifier.eissn1097-4164-
dc.identifier.piiS1097-2765(13)00407-3-
dc.description.statusPeer-revieweden
dc.description.versionPublisher Versionen
dc.type.subtypeJournal Article;Research Support, Non-U.S. Gov't-
pubs.organisational-group/Organisationen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGYen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciencesen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciences/Department of Biochemistryen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/Themesen
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/Themes/Canceren
pubs.organisational-group/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/Themes/Molecular & Cellular Bioscienceen
Appears in Collections:Published Articles, Dept. of Biochemistry

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