N-linked glycoproteome profiling of seedling leaf in brachypodium distachyon L.

Ming Zhang, Guan Xing Chen, Dong Wen Lv, Xiao Hui Li, Yue Ming Yan

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

Brachypodium distachyon L., a model plant for cereal crops, has become important as an alternative and potential biofuel grass. In plants, N-glycosylation is one of the most common and important protein modifications, playing important roles in signal recognition, increase in protein activity, stability of protein structure, and formation of tissues and organs. In this study, we performed the first glycoproteome analysis in the seedling leaves of B. distachyon. Using lectin affinity chromatography enrichment and mass-spectrometry-based analysis, we identified 47 glycosylation sites representing 46 N-linked glycoproteins. Motif-X analysis showed that two conserved motifs, N-X-T/S (X is any amino acid, except Pro), were significantly enriched. Further functional analysis suggested that some of these identified glycoproteins are involved in signal transduction, protein trafficking, and quality control and the modification and remodeling of cell-wall components such as receptor-like kinases, protein disulfide isomerase, and polygalacturonase. Moreover, transmembrane helices and signal peptide prediction showed that most of these glycoproteins could participate in typical protein secretory pathways in eukaryotes. The results provide a general overview of protein N-glycosylation modifications during the early growth of seedling leaves in B. distachyon and supplement the glycoproteome databases of plants.

Original languageEnglish (US)
Pages (from-to)1727-1738
Number of pages12
JournalJournal of Proteome Research
Volume14
Issue number4
DOIs
StatePublished - Apr 3 2015
Externally publishedYes

Keywords

  • Brachypodium distachyon
  • glycoproteome
  • glycosylation motif
  • leaf
  • lectin affinity chromatography enrichment

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

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