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Article: Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach

TitleIdentification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach
Authors
Issue Date2014
Citation
eLife, 2014, v. 3, article no. e02999 How to Cite?
AbstractPosttranslational modifications (PTMs) play a crucial role in a wide range of biological processes. Lysine crotonylation (Kcr) is a newly discovered histone PTM that is enriched at active gene promoters and potential enhancers in mammalian cell genomes. However, the cellular enzymes that regulate the addition and removal of Kcr are unknown, which has hindered further investigation of its cellular functions. Here we used a chemical proteomics approach to comprehensively profile 'eraser' enzymes that recognize a lysine-4 crotonylated histone H3 (H3K4Cr) mark. We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins. More importantly, Sirt3 functions as a decrotonylase to regulate histone Kcr dynamics and gene transcription in living cells. This discovery not only opens opportunities for examining the physiological significance of histone Kcr, but also helps to unravel the unknown cellular mechanisms controlled by Sirt3, that have previously been considered solely as a deacetylase.
Persistent Identifierhttp://hdl.handle.net/10722/206787
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorBao, Xen_US
dc.contributor.authorWang, Yen_US
dc.contributor.authorLi, Xen_US
dc.contributor.authorLi, Xen_US
dc.contributor.authorLiu, Zen_US
dc.contributor.authorYang, Ten_US
dc.contributor.authorWong, CFen_US
dc.contributor.authorZhang, Jen_US
dc.contributor.authorHao, Qen_US
dc.contributor.authorLi, Xen_US
dc.date.accessioned2014-12-02T09:17:48Z-
dc.date.available2014-12-02T09:17:48Z-
dc.date.issued2014en_US
dc.identifier.citationeLife, 2014, v. 3, article no. e02999en_US
dc.identifier.urihttp://hdl.handle.net/10722/206787-
dc.description.abstractPosttranslational modifications (PTMs) play a crucial role in a wide range of biological processes. Lysine crotonylation (Kcr) is a newly discovered histone PTM that is enriched at active gene promoters and potential enhancers in mammalian cell genomes. However, the cellular enzymes that regulate the addition and removal of Kcr are unknown, which has hindered further investigation of its cellular functions. Here we used a chemical proteomics approach to comprehensively profile 'eraser' enzymes that recognize a lysine-4 crotonylated histone H3 (H3K4Cr) mark. We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins. More importantly, Sirt3 functions as a decrotonylase to regulate histone Kcr dynamics and gene transcription in living cells. This discovery not only opens opportunities for examining the physiological significance of histone Kcr, but also helps to unravel the unknown cellular mechanisms controlled by Sirt3, that have previously been considered solely as a deacetylase.-
dc.languageengen_US
dc.relation.ispartofeLifeen_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleIdentification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approachen_US
dc.typeArticleen_US
dc.identifier.emailWang, Y: wyhku83@hku.hken_US
dc.identifier.emailWong, CF: cfwonghk@hku.hken_US
dc.identifier.emailZhang, J: jzhang1@hku.hken_US
dc.identifier.emailHao, Q: qhao@hku.hken_US
dc.identifier.emailLi, X: xiangli@hku.hken_US
dc.identifier.authorityZhang, J=rp01713en_US
dc.identifier.authorityHao, Q=rp01332en_US
dc.identifier.authorityLi, X=rp01562en_US
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.7554/eLife.02999en_US
dc.identifier.pmid25369635-
dc.identifier.pmcid4358366-
dc.identifier.hkuros241503en_US
dc.identifier.volume3en_US

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