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Article: A chemical reporter facilitates the detection and identification of lysine HMGylation on histones

TitleA chemical reporter facilitates the detection and identification of lysine HMGylation on histones
Authors
Issue Date2018
PublisherRoyal Society of Chemistry: Open Access Journals. The Journal's web site is located at http://www.rsc.org/publishing/journals/sc/About.asp
Citation
Chemical Science, 2018, v. 9 n. 40, p. 7797-7801 How to Cite?
AbstractLysine 3-hydroxyl-3-methylglutarylation (HMG-K) is a newly identified PTM that can occur non-enzymatically in mitochondria. However, the substrate scope of this new PTM remains insufficiently explored, which has greatly hindered the progress in interpreting its regulatory mechanisms and cellular functions. Here, we report the development of an alkyne-functionalized chemical reporter (HMGAM-yne), for the detection and identification of cellular HMGylated proteins. HMGAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent biorthogonal conjugation enables fluorescence visualization and identification of the protein substrates of HMG-K. Using HMGAM-yne, we also identified Sirt5 as an ‘eraser’ that regulates HMGylation in cells. In addition to the known mitochondrial HMG-K proteins, HMGAM-yne facilitates the discovery of multiple nuclear proteins, including histones, as novel substrates of lysine HMGylation.
Persistent Identifierhttp://hdl.handle.net/10722/263984
ISSN
2023 Impact Factor: 7.6
2023 SCImago Journal Rankings: 2.333
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBao, X-
dc.contributor.authorXiong, Y-
dc.contributor.authorLi, X-
dc.contributor.authorLi, XD-
dc.date.accessioned2018-10-22T07:47:39Z-
dc.date.available2018-10-22T07:47:39Z-
dc.date.issued2018-
dc.identifier.citationChemical Science, 2018, v. 9 n. 40, p. 7797-7801-
dc.identifier.issn2041-6520-
dc.identifier.urihttp://hdl.handle.net/10722/263984-
dc.description.abstractLysine 3-hydroxyl-3-methylglutarylation (HMG-K) is a newly identified PTM that can occur non-enzymatically in mitochondria. However, the substrate scope of this new PTM remains insufficiently explored, which has greatly hindered the progress in interpreting its regulatory mechanisms and cellular functions. Here, we report the development of an alkyne-functionalized chemical reporter (HMGAM-yne), for the detection and identification of cellular HMGylated proteins. HMGAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent biorthogonal conjugation enables fluorescence visualization and identification of the protein substrates of HMG-K. Using HMGAM-yne, we also identified Sirt5 as an ‘eraser’ that regulates HMGylation in cells. In addition to the known mitochondrial HMG-K proteins, HMGAM-yne facilitates the discovery of multiple nuclear proteins, including histones, as novel substrates of lysine HMGylation.-
dc.languageeng-
dc.publisherRoyal Society of Chemistry: Open Access Journals. The Journal's web site is located at http://www.rsc.org/publishing/journals/sc/About.asp-
dc.relation.ispartofChemical Science-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleA chemical reporter facilitates the detection and identification of lysine HMGylation on histones-
dc.typeArticle-
dc.identifier.emailBao, X: baoxc@hku.hk-
dc.identifier.emailLi, X: lx418@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityBao, X=rp02881-
dc.identifier.authorityLi, XD=rp01562-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/c8sc02483a-
dc.identifier.pmid30429988-
dc.identifier.pmcidPMC6194501-
dc.identifier.scopuseid_2-s2.0-85055334572-
dc.identifier.hkuros293756-
dc.identifier.volume9-
dc.identifier.issue40-
dc.identifier.spage7797-
dc.identifier.epage7801-
dc.identifier.isiWOS:000448407600004-
dc.publisher.placeUnited Kingdom-
dc.identifier.issnl2041-6520-

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