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Article: Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2–nucleosome association

TitleLysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2–nucleosome association
Authors
Issue Date2021
PublisherRoyal Society of Chemistry: Open Access Journals. The Journal's web site is located at https://www.rsc.org/journals-books-databases/about-journals/rsc-chemical-biology/
Citation
RSC Chemical Biology, 2021, v. 2 n. 4, p. 1257-1262 How to Cite?
AbstractLysine succinylation (Ksucc) is a novel posttranslational modification that frequently occurs on chromatin proteins including histones and non-histone proteins. Histone Ksucc affects nucleosome dynamics by increasing the DNA unwrapping rate and accessibility. However, very little is known about the regulation and functions of Ksucc located on non-histone chromosomal proteins. Here, we site-specifically installed a succinyl lysine analogue (Kcsucc) onto the non-histone chromosomal protein HMG-17 (HMGN2) to mimic the natural succinylated protein. We found that the incorporation of Kcsucc into HMGN2 at the K30 site (HMGN2Kc30succ), which is located within the nucleosome-binding domain (NBD), leads to significantly decreased HMGN2 binding to the mononucleosome. HMGN2Kc30succ also increased the nucleosomal DNA accessibility by promoting nucleosomal DNA unwrapping in the entry/exit region. This study reveals a novel mechanism of non-histone protein succinylation on altering chromatin recruitment, which can further affect nucleosome and chromatin dynamics.
Persistent Identifierhttp://hdl.handle.net/10722/306487
ISSN
2023 Impact Factor: 4.2
2023 SCImago Journal Rankings: 1.144
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorJING, Y-
dc.contributor.authorTian, G-
dc.contributor.authorQIN, X-
dc.contributor.authorLiu, Z-
dc.contributor.authorLi, XD-
dc.date.accessioned2021-10-22T07:35:19Z-
dc.date.available2021-10-22T07:35:19Z-
dc.date.issued2021-
dc.identifier.citationRSC Chemical Biology, 2021, v. 2 n. 4, p. 1257-1262-
dc.identifier.issn2633-0679-
dc.identifier.urihttp://hdl.handle.net/10722/306487-
dc.description.abstractLysine succinylation (Ksucc) is a novel posttranslational modification that frequently occurs on chromatin proteins including histones and non-histone proteins. Histone Ksucc affects nucleosome dynamics by increasing the DNA unwrapping rate and accessibility. However, very little is known about the regulation and functions of Ksucc located on non-histone chromosomal proteins. Here, we site-specifically installed a succinyl lysine analogue (Kcsucc) onto the non-histone chromosomal protein HMG-17 (HMGN2) to mimic the natural succinylated protein. We found that the incorporation of Kcsucc into HMGN2 at the K30 site (HMGN2Kc30succ), which is located within the nucleosome-binding domain (NBD), leads to significantly decreased HMGN2 binding to the mononucleosome. HMGN2Kc30succ also increased the nucleosomal DNA accessibility by promoting nucleosomal DNA unwrapping in the entry/exit region. This study reveals a novel mechanism of non-histone protein succinylation on altering chromatin recruitment, which can further affect nucleosome and chromatin dynamics.-
dc.languageeng-
dc.publisherRoyal Society of Chemistry: Open Access Journals. The Journal's web site is located at https://www.rsc.org/journals-books-databases/about-journals/rsc-chemical-biology/-
dc.relation.ispartofRSC Chemical Biology-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleLysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2–nucleosome association-
dc.typeArticle-
dc.identifier.emailTian, G: tiangf@connect.hku.hk-
dc.identifier.emailLiu, Z: lz2021@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityLi, XD=rp01562-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/D1CB00070E-
dc.identifier.pmid34458839-
dc.identifier.pmcidPMC8341127-
dc.identifier.scopuseid_2-s2.0-85112218561-
dc.identifier.hkuros329014-
dc.identifier.volume2-
dc.identifier.issue4-
dc.identifier.spage1257-
dc.identifier.epage1262-
dc.identifier.isiWOS:000663009600001-
dc.publisher.placeUnited Kingdom-

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