Proceedings of the National Academy of Sciences · 2017 · 123 citations · 60 references
Life SciencesBiochemistryPlant BiologyGlycobiologyPlant BiochemistryPlant Molecular BiologyGlycosylation PathwaysN-linked GlycosylationO-linked GlycosylationPlant EnzymesPlant GlycobiologyPlant ProteomicsDevelopmental Roles Of O-glycosylationN-acetylglucosamine LabelingO-glcnacylation In DevelopmentO-glycosylation In PlantsO-linked N-acetylglucosamine ModificationPost-translational Modification SitesProtein Glycosylation PathwaysSite-specific O-glycoproteomics
Using lectin weak affinity chromatography to enrich modified peptides, followed by mass spectrometry, we identified 971 O-GlcNAc-modified peptides belonging to 262 proteins. The modified proteins are involved in cellular regulatory processes, including transcription, translation, epigenetic gene regulation, and signal transduction. Many proteins have functions in developmental and physiological processes specific to plants, such as hormone responses and flower development. Mass spectrometric analysis of phosphopeptides from the same samples showed that a large number of peptides could be modified by either O-GlcNAcylation or phosphorylation, but cooccurrence of the two modifications in the same peptide molecule was rare. Our study generates a snapshot of the O-GlcNAc modification landscape in plants, indicating functions in many cellular regulation pathways and providing a powerful resource for further dissecting these functions at the molecular level.
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N6-methyladenosine-dependent regulation of messenger RNA stability
Xiao Wang, Zhike Lu, Adrian Gomez-Nguyen et al. · Nature · 2013 · 4.8K citations
Raheel Shafi, Sai Prasad N. Iyer, Lesley G. Ellies et al. · Proceedings of the National Academy of Sciences · 2000 · 795 citations