Reader domain specificity and lysine demethylase-4 family function

Simple item page
dc.citation.articleNumber13387en_US
dc.citation.journalTitleNature Communicationsen_US
dc.citation.volumeNumber7en_US
dc.contributor.authorSu, Zhanglien_US
dc.contributor.authorWang, Fengbinen_US
dc.contributor.authorLee, Jin-Heeen_US
dc.contributor.authorStephens, Kimberly E.en_US
dc.contributor.authorPapazyan, Romeoen_US
dc.contributor.authorVoronina, Ekaterinaen_US
dc.contributor.authorKrautkramer, Kimberly A.en_US
dc.contributor.authorRaman, Anaen_US
dc.contributor.authorThorpe, Jeremy J.en_US
dc.contributor.authorBoersma, Melissa D.en_US
dc.contributor.authorKuznetsov, Vyacheslav I.en_US
dc.contributor.authorMiller, Mitchell D.en_US
dc.contributor.authorTaverna, Sean D.en_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.contributor.authorDenu, John M.en_US
dc.date.accessioned2016-12-01T17:29:09Zen_US
dc.date.available2016-12-01T17:29:09Zen_US
dc.date.issued2016en_US
dc.description.abstractThe KDM4 histone demethylases are conserved epigenetic regulators linked to development, spermatogenesis and tumorigenesis. However, how the KDM4 family targets specific chromatin regions is largely unknown. Here, an extensive histone peptide microarray analysis uncovers trimethyl-lysine histone-binding preferences among the closely related KDM4 double tudor domains (DTDs). KDM4A/B DTDs bind strongly to H3K23me3, a poorly understood histone modification recently shown to be enriched in meiotic chromatin of ciliates and nematodes. The 2.28 Å co-crystal structure of KDM4A-DTD in complex with H3K23me3 peptide reveals key intermolecular interactions for H3K23me3 recognition. Furthermore, analysis of the 2.56 Å KDM4B-DTD crystal structure pinpoints the underlying residues required for exclusive H3K23me3 specificity, an interaction supported by in vivo co-localization of KDM4B and H3K23me3 at heterochromatin in mammalian meiotic and newly postmeiotic spermatocytes. In vitrodemethylation assays suggest H3K23me3 binding by KDM4B stimulates H3K36 demethylation. Together, these results provide a possible mechanism whereby H3K23me3-binding by KDM4B directs localized H3K36 demethylation during meiosis and spermatogenesis.en_US
dc.identifier.citationSu, Zhangli, Wang, Fengbin, Lee, Jin-Hee, et al.. "Reader domain specificity and lysine demethylase-4 family function." <i>Nature Communications,</i> 7, (2016) Springer Nature: http://dx.doi.org/10.1038/ncomms13387.en_US
dc.identifier.doihttp://dx.doi.org/10.1038/ncomms13387en_US
dc.identifier.urihttps://hdl.handle.net/1911/92734en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsThis work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material.en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.titleReader domain specificity and lysine demethylase-4 family functionen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
ncomms13387.pdf
Size:
1.77 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Faculty Publications
BioSciences Publications
Chemistry Publications