Journal
PLOS BIOLOGY
Volume 19, Issue 6, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pbio.3001277
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Funding
- German Research Foundation (DFG Postdoctoral Fellowship) [398625447]
- National Science Foundation [1817518]
- National Institute of Health (NIH) [AI118891]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1817518] Funding Source: National Science Foundation
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This study extended the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provided a detailed glycoproteome for this model archaeon. Through in-depth glycoproteomic analyses, the largest archaeal glycoproteome described so far was identified, revealing the complexity of N-glycosylation pathways in archaeal cell biology.
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. We further show that different N-glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx. volcanii N-glycoproteome revealed here provide new insights into the roles of N-glycosylation in archaeal cell biology.
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