{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schulze S"],"funding":["Deutsche Forschungsgemeinschaft","NIAID NIH HHS","Foundation for the National Institutes of Health","NCI NIH HHS","National Science Foundation"],"pagination":["e3001277"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8241124"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(6)"],"pubmed_abstract":["Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far."],"journal":["PLoS biology"],"pubmed_title":["Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea."],"pmcid":["PMC8241124"],"funding_grant_id":["398625447","1817518","P01 CA196539","AI118891","R01 AI118891"],"pubmed_authors":["Schulze S","Pohlschroder M","Pfeiffer F","Garcia BA"],"additional_accession":[]},"is_claimable":false,"name":"Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea.","description":"Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Jun","modification":"2026-05-07T22:28:59.161Z","creation":"2025-06-01T00:34:15.509Z"},"accession":"S-EPMC8241124","cross_references":{"pubmed":["34138841"],"doi":["10.1371/journal.pbio.3001277"]}}