Publication Information
Xu et al., 2016
Abstract
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.
Xu SL(1), Medzihradszky KF(2), Wang ZY(3), Burlingame AL(2), Chalkley RJ(4).
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.
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.
© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI: 10.1074/mcp.M115.056101
PMCID: PMC5083099
PMID: 27067053 [Indexed for MEDLINE]
