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Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea

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Pfeiffer,  Friedhelm
Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Schulze, S., Pfeiffer, F., Garcia, B. A., & Pohlschroder, M. (2021). Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea. PLoS Biology, 19(6): e3001277. doi:10.1371/journal.pbio.3001277.


Cite as: http://hdl.handle.net/21.11116/0000-0008-F410-2
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. 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.