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Article: Semisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility

TitleSemisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility
Authors
Issue Date2020
PublisherOxford University Press (OUP): Policy C - Option B. The Journal's web site is located at http://nar.oxfordjournals.org/
Citation
Nucleic Acids Research, 2020, Epub 2020-08-07 How to Cite?
AbstractPosttranslational modifications (PTMs) of histones represent a crucial regulatory mechanism of nucleosome and chromatin dynamics in various of DNA-based cellular processes, such as replication, transcription and DNA damage repair. Lysine succinylation (Ksucc) is a newly identified histone PTM, but its regulation and function in chromatin remain poorly understood. Here, we utilized an expressed protein ligation (EPL) strategy to synthesize histone H4 with site-specific succinylation at K77 residue (H4K77succ), an evolutionarily conserved succinylation site at the nucleosomal DNA-histone interface. We then assembled mononucleosomes with the semisynthetic H4K77succ in vitro. We demonstrated that this succinylation impacts nucleosome dynamics and promotes DNA unwrapping from the histone surface, which allows proteins such as transcription factors to rapidly access buried regions of the nucleosomal DNA. In budding yeast, a lysine-to-glutamic acid mutation, which mimics Ksucc, at the H4K77 site reduced nucleosome stability and led to defects in DNA damage repair and telomere silencing in vivo. Our findings revealed this uncharacterized histone modification has important roles in nucleosome and chromatin dynamics.
Persistent Identifierhttp://hdl.handle.net/10722/285416
ISSN
2019 Impact Factor: 11.501
2015 SCImago Journal Rankings: 7.458

 

DC FieldValueLanguage
dc.contributor.authorJing, Y-
dc.contributor.authorDing, D-
dc.contributor.authorTian, G-
dc.contributor.authorKwan, KCJ-
dc.contributor.authorLiu, Z-
dc.contributor.authorIshibashi, T-
dc.contributor.authorLi, XD-
dc.date.accessioned2020-08-18T03:53:14Z-
dc.date.available2020-08-18T03:53:14Z-
dc.date.issued2020-
dc.identifier.citationNucleic Acids Research, 2020, Epub 2020-08-07-
dc.identifier.issn0305-1048-
dc.identifier.urihttp://hdl.handle.net/10722/285416-
dc.description.abstractPosttranslational modifications (PTMs) of histones represent a crucial regulatory mechanism of nucleosome and chromatin dynamics in various of DNA-based cellular processes, such as replication, transcription and DNA damage repair. Lysine succinylation (Ksucc) is a newly identified histone PTM, but its regulation and function in chromatin remain poorly understood. Here, we utilized an expressed protein ligation (EPL) strategy to synthesize histone H4 with site-specific succinylation at K77 residue (H4K77succ), an evolutionarily conserved succinylation site at the nucleosomal DNA-histone interface. We then assembled mononucleosomes with the semisynthetic H4K77succ in vitro. We demonstrated that this succinylation impacts nucleosome dynamics and promotes DNA unwrapping from the histone surface, which allows proteins such as transcription factors to rapidly access buried regions of the nucleosomal DNA. In budding yeast, a lysine-to-glutamic acid mutation, which mimics Ksucc, at the H4K77 site reduced nucleosome stability and led to defects in DNA damage repair and telomere silencing in vivo. Our findings revealed this uncharacterized histone modification has important roles in nucleosome and chromatin dynamics.-
dc.languageeng-
dc.publisherOxford University Press (OUP): Policy C - Option B. The Journal's web site is located at http://nar.oxfordjournals.org/-
dc.relation.ispartofNucleic Acids Research-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleSemisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility-
dc.typeArticle-
dc.identifier.emailTian, G: tiangf@hku.hk-
dc.identifier.emailLiu, Z: lz0418@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityLi, XD=rp01562-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1093/nar/gkaa663-
dc.identifier.scopuseid_2-s2.0-85091691642-
dc.identifier.hkuros312792-
dc.identifier.volumeEpub 2020-08-07-
dc.publisher.placeUnited Kingdom-

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