{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ostrowski A"],"funding":["Medical Research Council","University of Dundee","Wellcome Trust"],"pagination":["30291-305"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4683255"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["290(51)"],"pubmed_abstract":["Post-translational modification of proteins is a ubiquitous mechanism of signal transduction in all kingdoms of life. One such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, known as O-GlcNAcylation. This unusual type of glycosylation is thought to be restricted to nucleocytoplasmic proteins of eukaryotes and is mediated by a pair of O-GlcNAc-transferase and O-GlcNAc hydrolase enzymes operating on a large number of substrate proteins. Protein O-GlcNAcylation is responsive to glucose and flux through the hexosamine biosynthetic pathway. Thus, a close relationship is thought to exist between the level of O-GlcNAc proteins within and the general metabolic state of the cell. Although isolated apparent orthologues of these enzymes are present in bacter"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum."],"pmcid":["PMC4683255"],"funding_grant_id":["WT050558","WT087590MA","MR/M004139/1","TMRF PhD Fellowship","087590","G0900138"],"pubmed_authors":["Gundogdu M","van Aalten DM","Lebedev AA","Ostrowski A","Ferenbach AT"],"additional_accession":[]},"is_claimable":false,"name":"Evidence for a Functional O-Linked N-Acetylglucosamine (O-GlcNAc) System in the Thermophilic Bacterium Thermobaculum terrenum.","description":"Post-translational modification of proteins is a ubiquitous mechanism of signal transduction in all kingdoms of life. One such modification is addition of O-linked N-acetylglucosamine to serine or threonine residues, known as O-GlcNAcylation. This unusual type of glycosylation is thought to be restricted to nucleocytoplasmic proteins of eukaryotes and is mediated by a pair of O-GlcNAc-transferase and O-GlcNAc hydrolase enzymes operating on a large number of substrate proteins. Protein O-GlcNAcylation is responsive to glucose and flux through the hexosamine biosynthetic pathway. Thus, a close relationship is thought to exist between the level of O-GlcNAc proteins within and the general metabolic state of the cell. Although isolated apparent orthologues of these enzymes are present in bacter","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Dec","modification":"2025-04-19T17:50:23.039Z","creation":"2019-03-27T02:05:24Z"},"accession":"S-EPMC4683255","cross_references":{"pubmed":["26491011"],"doi":["10.1074/jbc.M115.689596"]}}