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- Publisher Website: 10.1016/j.molcel.2019.08.018
- Scopus: eid_2-s2.0-85072265694
- PMID: 31542297
- WOS: WOS:000497994500011
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Article: Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics
Title | Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics |
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Authors | |
Keywords | Histone lysine glutarylation Epigenetics Nucleosome dynamics Sirt7 KAT2A α-KADH DNA damage Chromatin condensation Chemical reporter |
Issue Date | 2019 |
Publisher | Cell 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? |
Abstract | Histone 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 Identifier | http://hdl.handle.net/10722/278065 |
ISSN | 2023 Impact Factor: 14.5 2023 SCImago Journal Rankings: 9.332 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Bao, X | - |
dc.contributor.author | Liu, Z | - |
dc.contributor.author | Zhang, W | - |
dc.contributor.author | Gladysz, KA | - |
dc.contributor.author | Fung, EYM | - |
dc.contributor.author | Tian, G | - |
dc.contributor.author | Xiong, Y | - |
dc.contributor.author | Wong, WHJ | - |
dc.contributor.author | Yuen, KWY | - |
dc.contributor.author | Li, XD | - |
dc.date.accessioned | 2019-10-04T08:06:49Z | - |
dc.date.available | 2019-10-04T08:06:49Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Molecular Cell, 2019, v. 76 n. 4, p. 660-675.e9 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | http://hdl.handle.net/10722/278065 | - |
dc.description.abstract | Histone 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.language | eng | - |
dc.publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel | - |
dc.relation.ispartof | Molecular Cell | - |
dc.subject | Histone lysine glutarylation | - |
dc.subject | Epigenetics | - |
dc.subject | Nucleosome dynamics | - |
dc.subject | Sirt7 | - |
dc.subject | KAT2A | - |
dc.subject | α-KADH | - |
dc.subject | DNA damage | - |
dc.subject | Chromatin condensation | - |
dc.subject | Chemical reporter | - |
dc.title | Glutarylation of Histone H4 Lysine 91 Regulates Chromatin Dynamics | - |
dc.type | Article | - |
dc.identifier.email | Bao, X: baoxc@hku.hk | - |
dc.identifier.email | Liu, Z: lz0418@hku.hk | - |
dc.identifier.email | Zhang, W: zw513@hku.hk | - |
dc.identifier.email | Gladysz, KA: kornelia@hku.hk | - |
dc.identifier.email | Fung, EYM: eva.fungym@hku.hk | - |
dc.identifier.email | Tian, G: gftian@HKUCC-COM.hku.hk | - |
dc.identifier.email | Wong, WHJ: jwhwong@hku.hk | - |
dc.identifier.email | Yuen, KWY: kwyyuen@hku.hk | - |
dc.identifier.email | Li, XD: xiangli@hku.hk | - |
dc.identifier.authority | Fung, EYM=rp01986 | - |
dc.identifier.authority | Wong, WHJ=rp02363 | - |
dc.identifier.authority | Yuen, KWY=rp01512 | - |
dc.identifier.authority | Li, XD=rp01562 | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/j.molcel.2019.08.018 | - |
dc.identifier.pmid | 31542297 | - |
dc.identifier.scopus | eid_2-s2.0-85072265694 | - |
dc.identifier.hkuros | 306150 | - |
dc.identifier.volume | 76 | - |
dc.identifier.issue | 4 | - |
dc.identifier.spage | 660 | - |
dc.identifier.epage | 675.e9 | - |
dc.identifier.isi | WOS:000497994500011 | - |
dc.publisher.place | United States | - |
dc.identifier.f1000 | 736645685 | - |
dc.identifier.issnl | 1097-2765 | - |