{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["El Qaidi S"],"funding":["National Institute of Allergy and Infectious Diseases","NIAID NIH HHS","ARC Discovery Project Grant","National Institute of General Medical Sciences","NIGMS NIH HHS","Australian Research Council Future Fellowship"],"pagination":["5293"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8964723"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(1)"],"pubmed_abstract":["The Salmonella enterica SseK1 protein is a type three secretion system effector that glycosylates host proteins during infection on specific arginine residues with N-acetyl glucosamine (GlcNAc). SseK1 also Arg-glycosylates endogenous bacterial proteins and we thus hypothesized that SseK1 activities might be integrated with regulating the intrabacterial abundance of UPD-GlcNAc, the sugar-nucleotide donor used by this effector. After searching for new SseK1 substrates, we found that SseK1 glycosylates arginine residues in the dual repressor-activator protein NagC, leading to increased DNA-binding affinity and enhanced expression of the NagC-regulated genes glmU and glmS. SseK1 also glycosylates arginine residues in GlmR, a protein that enhances GlmS activity. This Arg-glycosylation improves "],"journal":["Scientific reports"],"pubmed_title":["Arginine glycosylation regulates UDP-GlcNAc biosynthesis in Salmonella enterica."],"pmcid":["PMC8964723"],"funding_grant_id":["P20GM130448","R21 AI168453","FT200100270","AI127973","DP210100362"],"pubmed_authors":["Scott NE","Hays MP","Hardwidge PR","El Qaidi S"],"additional_accession":[]},"is_claimable":false,"name":"Arginine glycosylation regulates UDP-GlcNAc biosynthesis in Salmonella enterica.","description":"The Salmonella enterica SseK1 protein is a type three secretion system effector that glycosylates host proteins during infection on specific arginine residues with N-acetyl glucosamine (GlcNAc). SseK1 also Arg-glycosylates endogenous bacterial proteins and we thus hypothesized that SseK1 activities might be integrated with regulating the intrabacterial abundance of UPD-GlcNAc, the sugar-nucleotide donor used by this effector. After searching for new SseK1 substrates, we found that SseK1 glycosylates arginine residues in the dual repressor-activator protein NagC, leading to increased DNA-binding affinity and enhanced expression of the NagC-regulated genes glmU and glmS. SseK1 also glycosylates arginine residues in GlmR, a protein that enhances GlmS activity. This Arg-glycosylation improves ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Mar","modification":"2025-05-29T19:46:52.587Z","creation":"2025-04-05T07:15:35.989Z"},"accession":"S-EPMC8964723","cross_references":{"pubmed":["35351940"],"doi":["10.1038/s41598-022-09276-9"]}}