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Glycoproteomic analysis of Haloferax volcanii strains H53, DaglB, and Dagl15

ABSTRACT: An in-depth glycoproteomic analysis of Haloferax volcanii has been performed, comparing the wildtype H53 with knockout mutants of aglB and agl15. While AglB-dependent glycosylation has been described to occur under standard culture conditions, the Agl15-dependent glycosylation pathway has previously been described to be only active under low-salt conditions. In this dataset, the largest archaeal glycoproteome could be identified with more than 40 N-glycoproteins and more than 100 N-glycopptides. It reveals not only that both glycosylation pathways can be active under the same conditions but also that the same glycosites can be modified by different glycans from both glycosylation pathways.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Haloferax Volcanii (halobacterium Volcanii)

SUBMITTER: Stefan Schulze

LAB HEAD: Mechthild Pohlschroder

PROVIDER: PXD021874 | Pride | 2021-06-20

REPOSITORIES: Pride

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

Schulze Stefan S Pfeiffer Friedhelm F Garcia Benjamin A BA Pohlschroder Mechthild M

PLoS biology 20210617 6

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 th ...[more]

PMID: 34138841

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