{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":45,"searchCount":0},"additional":{"submitter":["Resto M"],"funding":["National Heart, Lung, and Blood Institute","National Cancer Institute"],"pagination":["22703-22713"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5077205"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["291(43)"],"pubmed_abstract":["We describe here the identification and functional characterization of the enzyme O-GlcNAcase (OGA) as an RNA polymerase II elongation factor. Using in vitro transcription elongation assays, we show that OGA activity is required for elongation in a crude nuclear extract system, whereas in a purified system devoid of OGA the addition of rOGA inhibited elongation. Furthermore, OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1β, and a purified OGA-SPT5-TIF1β complex has elongation properties. Lastly, ChIP-seq experiments show that OGA maps to the transcriptional start site/5' ends of genes, showing considerable overlap with RNA pol II, SPT5, TRIM28-KAP1-TIF1β, and O-GlcNAc itself. These data all point to OGA as a component of the RNA pol II elongation machinery regulating elongation genome-wide. Our results add a novel and unexpected dimension to the regulation of elongation by the insertion of O-GlcNAc cycling into the pol II elongation regulatory dynamics."],"journal":["The Journal of biological chemistry"],"pubmed_title":["O-GlcNAcase Is an RNA Polymerase II Elongation Factor Coupled to Pausing Factors SPT5 and TIF1β."],"pmcid":["PMC5077205"],"funding_grant_id":["Intramural Program"],"pubmed_authors":["Fernandez AG","Kim BH","Resto M","Zhao K","Lewis BA","Abraham BJ"],"view_count":["45"],"additional_accession":[]},"is_claimable":false,"name":"O-GlcNAcase Is an RNA Polymerase II Elongation Factor Coupled to Pausing Factors SPT5 and TIF1β.","description":"We describe here the identification and functional characterization of the enzyme O-GlcNAcase (OGA) as an RNA polymerase II elongation factor. Using in vitro transcription elongation assays, we show that OGA activity is required for elongation in a crude nuclear extract system, whereas in a purified system devoid of OGA the addition of rOGA inhibited elongation. Furthermore, OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1β, and a purified OGA-SPT5-TIF1β complex has elongation properties. Lastly, ChIP-seq experiments show that OGA maps to the transcriptional start site/5' ends of genes, showing considerable overlap with RNA pol II, SPT5, TRIM28-KAP1-TIF1β, and O-GlcNAc itself. These data all point to OGA as a component of the RNA pol II elongation machinery regulating elongation genome-wide. Our results add a novel and unexpected dimension to the regulation of elongation by the insertion of O-GlcNAc cycling into the pol II elongation regulatory dynamics.","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Oct","modification":"2024-11-21T08:06:14.15Z","creation":"2019-06-06T16:32:08Z"},"accession":"S-EPMC5077205","cross_references":{"pubmed":["27601472"],"doi":["10.1074/jbc.M116.751420","10.1074/jbc.m116.751420"]}}