{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hardiville S"],"funding":["NIDDK NIH HHS","NHLBI NIH HHS","NINDS NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["1143-1152.e7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7061307"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["77(5)"],"pubmed_abstract":["In eukaryotes, gene expression is performed by three RNA polymerases that are targeted to promoters by molecular complexes. A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription. Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP. We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA. Transcriptomic and metabolomic analyses of TBP<sup>T114A</sup> CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes. Lack of O-GlcNA"],"journal":["Molecular cell"],"pubmed_title":["TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation."],"pmcid":["PMC7061307"],"funding_grant_id":["P01 HL107153","R01 DK116746","R01 DK061671","R01 NS072241","R01 GM116891"],"pubmed_authors":["Wolfgang MJ","Hart GW","Han G","Ma J","Banerjee PS","Talbot CC","Hardiville S","Selen Alpergin ES","Smith DM","Hu P"],"additional_accession":[]},"is_claimable":false,"name":"TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.","description":"In eukaryotes, gene expression is performed by three RNA polymerases that are targeted to promoters by molecular complexes. A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription. Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP. We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA. Transcriptomic and metabolomic analyses of TBP<sup>T114A</sup> CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes. Lack of O-GlcNA","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Mar","modification":"2026-05-02T13:43:10.557Z","creation":"2021-03-07T08:16:52Z"},"accession":"S-EPMC7061307","cross_references":{"pubmed":["31866147"],"doi":["10.1016/j.molcel.2019.11.022"]}}