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N-linked Glycan Micro-heterogeneity in Glycoproteins of Arabidopsis.


ABSTRACT: N-glycosylation is one of the most common protein post-translational modifications in eukaryotes and has a relatively conserved core structure between fungi, animals and plants. In plants, the biosynthesis of N-glycans has been extensively studied with all the major biosynthetic enzymes characterized. However, few studies have applied advanced mass spectrometry to profile intact plant N-glycopeptides. In this study, we use hydrophilic enrichment, high-resolution tandem mass spectrometry with complementary and triggered fragmentation to profile Arabidopsis N-glycopeptides from microsomal membranes of aerial tissues. A total of 492 N-glycosites were identified from 324 Arabidopsis proteins with extensive N-glycan structural heterogeneity revealed through 1110 N-glycopeptides. To demonstrate the precision of the approach, we also profiled N-glycopeptides from the mutant (xylt) of ?-1,2-xylosyltransferase, an enzyme in the N-glycan biosynthetic pathway. This analysis represents the most comprehensive and unbiased collection of Arabidopsis N-glycopeptides revealing an unsurpassed level of detail on the micro-heterogeneity present in N-glycoproteins of Arabidopsis. Data are available via ProteomeXchange with identifier PXD006270.

SUBMITTER: Zeng W 

PROVIDER: S-EPMC5836367 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

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<i>N</i>-linked Glycan Micro-heterogeneity in Glycoproteins of Arabidopsis.

Zeng Wei W   Ford Kristina L KL   Bacic Antony A   Heazlewood Joshua L JL  

Molecular & cellular proteomics : MCP 20171213 3


<i>N</i>-glycosylation is one of the most common protein post-translational modifications in eukaryotes and has a relatively conserved core structure between fungi, animals and plants. In plants, the biosynthesis of <i>N</i>-glycans has been extensively studied with all the major biosynthetic enzymes characterized. However, few studies have applied advanced mass spectrometry to profile intact plant <i>N</i>-glycopeptides. In this study, we use hydrophilic enrichment, high-resolution tandem mass  ...[more]

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