Molecular Basis of KAT2A Selecting Acyl-CoA Cofactors for Histone Modifications

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dc.citation.articleNumber109en_US
dc.citation.journalTitleResearchen_US
dc.citation.volumeNumber6en_US
dc.contributor.authorLi, Shaen_US
dc.contributor.authorLi, Nanen_US
dc.contributor.authorHe, Jieen_US
dc.contributor.authorZhou, Runxinen_US
dc.contributor.authorLu, Zhiminen_US
dc.contributor.authorTao, Yizhi Janeen_US
dc.contributor.authorGuo, Yusong R.en_US
dc.contributor.authorWang, Yugangen_US
dc.date.accessioned2023-04-25T14:48:15Zen_US
dc.date.available2023-04-25T14:48:15Zen_US
dc.date.issued2023en_US
dc.description.abstractEmerging discoveries about undocumented acyltransferase activities of known histone acetyltransferases (HATs) advance our understandings in the regulation of histone modifications. However, the molecular basis of HATs selecting acyl coenzyme A (acyl-CoA) substrates for histone modification is less known. We here report that lysine acetyltransferase 2A (KAT2A) as an illustrative instance of HATs can selectively utilize acetyl-CoA, propionyl-CoA, butyryl-CoA, and succinyl-CoA to directly deposit 18 histone acylation hallmarks in nucleosome. By analyzing the co-crystal structures of the catalytic domain of KAT2A in complex with acetyl-CoA, propionyl-CoA, butyryl-CoA, malonyl-CoA, succinyl-CoA, and glutaryl-CoA, we conclude that the alternative substrate-binding pocket of KAT2A and the length and electrostatic features of the acyl chain cooperatively determine the selection of the acyl-CoA substrates by KAT2A. This study reveals the molecular basis underlying the pluripotency of HATs that selectively install acylation hallmarks in nucleosomes, which might serve as instrumental mechanism to precisely regulate histone acylation profiles in cells.en_US
dc.identifier.citationLi, Sha, Li, Nan, He, Jie, et al.. "Molecular Basis of KAT2A Selecting Acyl-CoA Cofactors for Histone Modifications." <i>Research,</i> 6, (2023) AAAS: https://doi.org/10.34133/research.0109.en_US
dc.identifier.digitalresearch-0109en_US
dc.identifier.doihttps://doi.org/10.34133/research.0109en_US
dc.identifier.urihttps://hdl.handle.net/1911/114847en_US
dc.language.isoengen_US
dc.publisherAAASen_US
dc.rightsDistributed under a Creative Commons Attribution License (CC BY 4.0).en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.titleMolecular Basis of KAT2A Selecting Acyl-CoA Cofactors for Histone Modificationsen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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