N-Glycopeptide Profiling in Arabidopsis Inflorescence.
Mol Cell Proteomics
; 15(6): 2048-54, 2016 06.
Article
en En
| MEDLINE
| ID: mdl-27067053
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.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Glicopéptidos
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Arabidopsis
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Proteínas de Arabidopsis
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Inflorescencia
Idioma:
En
Revista:
Mol Cell Proteomics
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
2016
Tipo del documento:
Article