{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["298(8)"],"submitter":["Kikuchi M"],"pubmed_abstract":["Acetylated lysine residues (Kac) in histones are recognized by epigenetic reader proteins, such as Yaf9, ENL, AF9, Taf14, and Sas5 (YEATS) domain-containing proteins. Human YEATS domains bind to the acetylated N-terminal tail of histone H3; however, their Kac-binding preferences at the level of the nucleosome are unknown. Through genetic code reprogramming, here, we established a nucleosome core particle (NCP) array containing histones that were acetylated at specific residues and used it to compare the Kac-binding preferences of human YEATS domains. We found that AF9-YEATS showed basal binding to the unmodified NCP and that it bound stronger to the NCP containing a single acetylation at one of K4, K9, K14, or K27 of H3, or to histone H4 multi-acetylated between K5 and K16. Crystal structu"],"journal":["The Journal of biological chemistry"],"pagination":["102164"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9293779"],"repository":["biostudies-literature"],"pubmed_title":["Elucidation of binding preferences of YEATS domains to site-specific acetylated nucleosome core particles."],"pmcid":["PMC9293779"],"pubmed_authors":["Kikuchi M","Wakamori M","Goto M","Umehara T","Morita S","Katsura K","Shirouzu M","Hanada K"],"additional_accession":[]},"is_claimable":false,"name":"Elucidation of binding preferences of YEATS domains to site-specific acetylated nucleosome core particles.","description":"Acetylated lysine residues (Kac) in histones are recognized by epigenetic reader proteins, such as Yaf9, ENL, AF9, Taf14, and Sas5 (YEATS) domain-containing proteins. Human YEATS domains bind to the acetylated N-terminal tail of histone H3; however, their Kac-binding preferences at the level of the nucleosome are unknown. Through genetic code reprogramming, here, we established a nucleosome core particle (NCP) array containing histones that were acetylated at specific residues and used it to compare the Kac-binding preferences of human YEATS domains. We found that AF9-YEATS showed basal binding to the unmodified NCP and that it bound stronger to the NCP containing a single acetylation at one of K4, K9, K14, or K27 of H3, or to histone H4 multi-acetylated between K5 and K16. Crystal structu","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-05-09T23:42:51.591Z","creation":"2025-04-04T22:12:11.131Z"},"accession":"S-EPMC9293779","cross_references":{"pubmed":["35732209"],"doi":["10.1016/j.jbc.2022.102164"]}}