Proteomics

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A Novel Two-Stage Tandem Mass Spectrometry Approach and Scoring Scheme for the Identification of O-GlcNAc Modified Peptides

ABSTRACT: The modification of serine and threonine residues in proteins by a single N-acetylglucosamine (O-GlcNAc) residue is an emerging post-translational modification (PTM) with broad biological implications. However, the systematic or large-scale analysis of this PTM is hampered by several factors, including low stoichiometry and the lability of the O-glycosidic bond during tandem mass spectrometry. Using a library of 72 synthetic glycopeptides, we developed a two-stage tandem MS approach consisting of pulsed Q dissociation (PQD) for O-GlcNAc peptide detection and electron transfer dissociation (ETD) for identification and site localization. Based on a set of O-GlcNAc specific fragment ions, we further developed a score (OScore) that discriminates O-GlcNAc peptide spectra from spectra of unmodified peptides with 95% sensitivity and >99% specificity. Integrating the OScore into the two-stage LC-MS/MS approach detected O-GlcNAc peptides in the low fmol range and at 10-fold better sensitivity than a single data-dependent ETD tandem MS experiment.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Hannes Hahne  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD010152 | Pride | 2018-06-18

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
TechDev_OGlcNAc_Spiking1000_1.RAW Raw
TechDev_OGlcNAc_Spiking1000_1.RAW.-1.mgf Mgf
TechDev_OGlcNAc_Spiking1000_1.RAW.-1.mgf.rnk.out Mgf
TechDev_OGlcNAc_Spiking1000_1.mzXML Mzxml
TechDev_OGlcNAc_Spiking1000_ETD_directID_1.RAW Raw
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Publications

A novel two-stage tandem mass spectrometry approach and scoring scheme for the identification of O-GlcNAc modified peptides.

Hahne Hannes H   Kuster Bernhard B  

Journal of the American Society for Mass Spectrometry 20110326 5

The modification of serine and threonine residues in proteins by a single N-acetylglucosamine (O-GlcNAc) residue is an emerging post-translational modification (PTM) with broad biological implications. However, the systematic or large-scale analysis of this PTM is hampered by several factors, including low stoichiometry and the lability of the O-glycosidic bond during tandem mass spectrometry. Using a library of 72 synthetic glycopeptides, we developed a two-stage tandem MS approach consisting o  ...[more]

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