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Article: Site-Specific Installation of Succinyl Lysine Analog into Histones Reveals the Effect of H2BK34 Succinylation on Nucleosome Dynamics

TitleSite-Specific Installation of Succinyl Lysine Analog into Histones Reveals the Effect of H2BK34 Succinylation on Nucleosome Dynamics
Authors
Issue Date2017
PublisherElsevier. The Journal's web site is located at http://www.cell.com/cell-chemical-biology/home
Citation
Cell Chemical Biology, 2017, v. 25, p. 166-174 How to Cite?
AbstractPosttranslational modifications of histones play key roles in the dynamic regulation of chromatin structure. Lysine succinylation is a new type of histone modification, but its biological significance in chromatin structure and dynamics remains unknown. Here we develop a chemical approach to site-specifically install a succinyl lysine analog into histones. This analog serves as an ideal structural and functional mimic to natural succinyl lysine. The incorporation of this succinylation mimic into histone H2B at lysine 34, a succinylation site at the nucleosomal DNA-histone interface, leads to significant decrease in nucleosome stability in vitro, which is consistent with the defects in chromatin structure of a budding yeast strain containing a lysine-to-glutamate mutation at the corresponding residue of yeast histone H2B. This study provides a simple method for the rapid generation of histones with site-specific succinylation mimics, and reveals novel regulatory mechanisms of histone succinylation in the dynamic organization of chromatin.
Persistent Identifierhttp://hdl.handle.net/10722/252117
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorJING, Y-
dc.contributor.authorLiu, Z-
dc.contributor.authorTIAN, G-
dc.contributor.authorIshibashi, TOYOTAKA-
dc.contributor.authorLi, XD-
dc.date.accessioned2018-04-11T01:17:09Z-
dc.date.available2018-04-11T01:17:09Z-
dc.date.issued2017-
dc.identifier.citationCell Chemical Biology, 2017, v. 25, p. 166-174-
dc.identifier.issn2451-9456-
dc.identifier.urihttp://hdl.handle.net/10722/252117-
dc.description.abstractPosttranslational modifications of histones play key roles in the dynamic regulation of chromatin structure. Lysine succinylation is a new type of histone modification, but its biological significance in chromatin structure and dynamics remains unknown. Here we develop a chemical approach to site-specifically install a succinyl lysine analog into histones. This analog serves as an ideal structural and functional mimic to natural succinyl lysine. The incorporation of this succinylation mimic into histone H2B at lysine 34, a succinylation site at the nucleosomal DNA-histone interface, leads to significant decrease in nucleosome stability in vitro, which is consistent with the defects in chromatin structure of a budding yeast strain containing a lysine-to-glutamate mutation at the corresponding residue of yeast histone H2B. This study provides a simple method for the rapid generation of histones with site-specific succinylation mimics, and reveals novel regulatory mechanisms of histone succinylation in the dynamic organization of chromatin.-
dc.languageeng-
dc.publisherElsevier. The Journal's web site is located at http://www.cell.com/cell-chemical-biology/home-
dc.relation.ispartofCell Chemical Biology-
dc.titleSite-Specific Installation of Succinyl Lysine Analog into Histones Reveals the Effect of H2BK34 Succinylation on Nucleosome Dynamics-
dc.typeArticle-
dc.identifier.emailLiu, Z: lz0418@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityLi, XD=rp01562-
dc.identifier.doi10.1016/j.chembiol.2017.11.005-
dc.identifier.scopuseid_2-s2.0-85039052737-
dc.identifier.hkuros284595-
dc.identifier.volume25-
dc.identifier.spage166-
dc.identifier.epage174-
dc.identifier.isiWOS:000425281100008-
dc.publisher.placeNetherlands-

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