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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
Keywordschromatin structure
crotonylation
histone modification
nucleosome
protein labelling
SIRT5
sirtuin
succinylation
thiol-ene reaction
Issue Date2018
PublisherElsevier. The Journal's web site is located at http://www.cell.com/cell-chemical-biology/home
Citation
Cell Chemical Biology, 2018, v. 25 n. 2, p. 166-174.e7 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
2023 Impact Factor: 6.6
2023 SCImago Journal Rankings: 2.584
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorJing, Y-
dc.contributor.authorLiu, Z-
dc.contributor.authorTian, G-
dc.contributor.authorBao, X-
dc.contributor.authorIshibashi, T-
dc.contributor.authorLi, XD-
dc.date.accessioned2018-04-11T01:17:09Z-
dc.date.available2018-04-11T01:17:09Z-
dc.date.issued2018-
dc.identifier.citationCell Chemical Biology, 2018, v. 25 n. 2, p. 166-174.e7-
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.subjectchromatin structure-
dc.subjectcrotonylation-
dc.subjecthistone modification-
dc.subjectnucleosome-
dc.subjectprotein labelling-
dc.subjectSIRT5-
dc.subjectsirtuin-
dc.subjectsuccinylation-
dc.subjectthiol-ene reaction-
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.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/j.chembiol.2017.11.005-
dc.identifier.pmid29249693-
dc.identifier.scopuseid_2-s2.0-85039052737-
dc.identifier.hkuros284595-
dc.identifier.volume25-
dc.identifier.issue2-
dc.identifier.spage166-
dc.identifier.epage174.e7-
dc.identifier.isiWOS:000425281100008-
dc.publisher.placeNetherlands-
dc.identifier.issnl2451-9448-

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