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Title: N-Glycopeptide Profiling in Arabidopsis Inflorescence

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 ETD 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 non-consensus glycosylation motifs. Finally, while most of the modified proteins are secreted, membrane, ER or Golgi localized proteins, surprisingly N-linked sugars were detected on a protein predicted to be cytosolic or nuclear.

Authors:
 [1];  [2];  [3];  [2];  [2]
  1. Carnegie Inst. of Science, Stanford, CA (United States). Dept. of Plant Biology; Univ. of California, San Francisco, CA (United States). Dept. of Pharmaceutical Chemistry
  2. Univ. of California, San Francisco, CA (United States). Dept. of Pharmaceutical Chemistry
  3. Carnegie Inst. of Science, Stanford, CA (United States). Dept. of Plant Biology
Publication Date:
Research Org.:
Carnegie Inst. of Washington, Washington, DC (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); Howard Hughes Medical Institute
OSTI Identifier:
1435028
Grant/Contract Number:  
FG02-08ER15973; NIGMS 8P41GM103481
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Molecular and Cellular Proteomics
Additional Journal Information:
Journal Volume: 15; Journal Issue: 6; Journal ID: ISSN 1535-9476
Publisher:
American Society for Biochemistry and Molecular Biology
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Arabidopsis; Glycoproteomics; N-Glycosylation; Plant Biology; Protein Modification; ETD; LWAC

Citation Formats

Xu, Shou-Ling, Medzihradszky, Katalin F., Wang, Zhi-Yong, Burlingame, Alma L., and Chalkley, Robert J. N-Glycopeptide Profiling in Arabidopsis Inflorescence. United States: N. p., 2016. Web. doi:10.1074/mcp.M115.056101.
Xu, Shou-Ling, Medzihradszky, Katalin F., Wang, Zhi-Yong, Burlingame, Alma L., & Chalkley, Robert J. N-Glycopeptide Profiling in Arabidopsis Inflorescence. United States. https://doi.org/10.1074/mcp.M115.056101
Xu, Shou-Ling, Medzihradszky, Katalin F., Wang, Zhi-Yong, Burlingame, Alma L., and Chalkley, Robert J. Mon . "N-Glycopeptide Profiling in Arabidopsis Inflorescence". United States. https://doi.org/10.1074/mcp.M115.056101. https://www.osti.gov/servlets/purl/1435028.
@article{osti_1435028,
title = {N-Glycopeptide Profiling in Arabidopsis Inflorescence},
author = {Xu, Shou-Ling and Medzihradszky, Katalin F. and Wang, Zhi-Yong and Burlingame, Alma L. and Chalkley, Robert J.},
abstractNote = {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 ETD 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 non-consensus glycosylation motifs. Finally, while most of the modified proteins are secreted, membrane, ER or Golgi localized proteins, surprisingly N-linked sugars were detected on a protein predicted to be cytosolic or nuclear.},
doi = {10.1074/mcp.M115.056101},
url = {https://www.osti.gov/biblio/1435028}, journal = {Molecular and Cellular Proteomics},
issn = {1535-9476},
number = 6,
volume = 15,
place = {United States},
year = {2016},
month = {4}
}

Journal Article:
Free Publicly Available Full Text
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Citation Metrics:
Cited by: 14 works
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Works referenced in this record:

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    Plant Lectins and Lectin Receptor-Like Kinases: How Do They Sense the Outside?
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