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Article: Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics

TitleGlutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics
Authors
Keywordshistone lysine glutarylation
epigenetics
nucleosome dynamics
Sirt7
KAT2A
Issue Date2019
PublisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel
Citation
Molecular Cell, 2019, v. 76 n. 4, p. 660-675.e9 How to Cite?
AbstractHistone posttranslational modifications (PTMs) regulate chromatin structure and dynamics during various DNA-associated processes. Here, we report that lysine glutarylation (Kglu) occurs at 27 lysine residues on human core histones. Using semi-synthetic glutarylated histones, we show that an evolutionarily conserved Kglu at histone H4K91 destabilizes nucleosome in vitro. In Saccharomyces cerevisiae, the replacement of H4K91 by glutamate that mimics Kglu influences chromatin structure and thereby results in a global upregulation of transcription and defects in cell-cycle progression, DNA damage repair, and telomere silencing. In mammalian cells, H4K91glu is mainly enriched at promoter regions of highly expressed genes. A downregulation of H4K91glu is tightly associated with chromatin condensation during mitosis and in response to DNA damage. The cellular dynamics of H4K91glu is controlled by Sirt7 as a deglutarylase and KAT2A as a glutaryltransferase. This study designates a new histone mark (Kglu) as a new regulatory mechanism for chromatin dynamics.
Persistent Identifierhttp://hdl.handle.net/10722/278065
ISSN
2017 Impact Factor: 14.248
2015 SCImago Journal Rankings: 13.658
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBao, X-
dc.contributor.authorLiu, Z-
dc.contributor.authorZhang, W-
dc.contributor.authorGladysz, KA-
dc.contributor.authorFung, EYM-
dc.contributor.authorTian, G-
dc.contributor.authorXiong, Y-
dc.contributor.authorWong, WHJ-
dc.contributor.authorYuen, KWY-
dc.contributor.authorLi, XD-
dc.date.accessioned2019-10-04T08:06:49Z-
dc.date.available2019-10-04T08:06:49Z-
dc.date.issued2019-
dc.identifier.citationMolecular Cell, 2019, v. 76 n. 4, p. 660-675.e9-
dc.identifier.issn1097-2765-
dc.identifier.urihttp://hdl.handle.net/10722/278065-
dc.description.abstractHistone posttranslational modifications (PTMs) regulate chromatin structure and dynamics during various DNA-associated processes. Here, we report that lysine glutarylation (Kglu) occurs at 27 lysine residues on human core histones. Using semi-synthetic glutarylated histones, we show that an evolutionarily conserved Kglu at histone H4K91 destabilizes nucleosome in vitro. In Saccharomyces cerevisiae, the replacement of H4K91 by glutamate that mimics Kglu influences chromatin structure and thereby results in a global upregulation of transcription and defects in cell-cycle progression, DNA damage repair, and telomere silencing. In mammalian cells, H4K91glu is mainly enriched at promoter regions of highly expressed genes. A downregulation of H4K91glu is tightly associated with chromatin condensation during mitosis and in response to DNA damage. The cellular dynamics of H4K91glu is controlled by Sirt7 as a deglutarylase and KAT2A as a glutaryltransferase. This study designates a new histone mark (Kglu) as a new regulatory mechanism for chromatin dynamics.-
dc.languageeng-
dc.publisherCell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel-
dc.relation.ispartofMolecular Cell-
dc.subjecthistone lysine glutarylation-
dc.subjectepigenetics-
dc.subjectnucleosome dynamics-
dc.subjectSirt7-
dc.subjectKAT2A-
dc.titleGlutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics-
dc.typeArticle-
dc.identifier.emailBao, X: baoxc@hku.hk-
dc.identifier.emailLiu, Z: lz0418@hku.hk-
dc.identifier.emailZhang, W: zw513@hku.hk-
dc.identifier.emailGladysz, KA: kornelia@hku.hk-
dc.identifier.emailFung, EYM: eva.fungym@hku.hk-
dc.identifier.emailTian, G: gftian@HKUCC-COM.hku.hk-
dc.identifier.emailWong, WHJ: jwhwong@hku.hk-
dc.identifier.emailYuen, KWY: kwyyuen@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityFung, EYM=rp01986-
dc.identifier.authorityWong, WHJ=rp02363-
dc.identifier.authorityYuen, KWY=rp01512-
dc.identifier.authorityLi, XD=rp01562-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.molcel.2019.08.018-
dc.identifier.pmid31542297-
dc.identifier.scopuseid_2-s2.0-85072265694-
dc.identifier.hkuros306150-
dc.identifier.volume76-
dc.identifier.issue4-
dc.identifier.spage660-
dc.identifier.epage675.e9-
dc.identifier.isiWOS:000497994500011-
dc.publisher.placeUnited States-
dc.identifier.f1000736645685-

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