Format

Send to

Choose Destination
Mol Cell Proteomics. 2016 Jun;15(6):2048-54. doi: 10.1074/mcp.M115.056101. Epub 2016 Apr 11.

N-Glycopeptide Profiling in Arabidopsis Inflorescence.

Author information

1
From the ‡Department of Plant Biology, Carnegie Institution for Science, Stanford, California 94305; §Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California 94143.
2
§Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California 94143.
3
From the ‡Department of Plant Biology, Carnegie Institution for Science, Stanford, California 94305;
4
§Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California 94143 chalkley@cgl.ucsf.edu.

Abstract

This study presents the first large-scale analysis of plant intact glycopeptides. Using wheat germ agglutinin lectin weak affinity chromatography to enrich modified peptides, followed by electron transfer dissociation (ETD)(1) fragmentation tandem mass spectrometry, glycan compositions on over 1100 glycopeptides from 270 proteins found in Arabidopsis inflorescence tissue were characterized. While some sites were only detected with a single glycan attached, others displayed up to 16 different glycoforms. Among the identified glycopeptides were four modified in nonconsensus glycosylation motifs. While most of the modified proteins are secreted, membrane, endoplasmic reticulum (ER), or Golgi-localized proteins, surprisingly, N-linked sugars were detected on a protein predicted to be cytosolic or nuclear.

PMID:
27067053
PMCID:
PMC5083099
DOI:
10.1074/mcp.M115.056101
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center