Glycosylation Proteomics Research Of Flower Bud And Leaf Bud From P. Simonii X P. Nigra

Glycosylation is an important way to post-translational modification of proteins, which affect protein structure, localization and biological activity. Glycosylated proteins play different roles in growth and development, fertilization recognition, and resistance responses of plants. Some studies suggest that some cell wall proteins in plants are glycosylated, but large-scale plants glycosylated protein separation and identification rarely reported. Poplar as an important mode plant of woody plants, the study about Populus buds and leaf buds glycosylated protein separation and identification of the main results obtained are as follows.By ConA-WGA-PNA-Jacalin lectin affinity chromatography to separate glycoproteins from male buds, female buds and leaf buds. Mass spectrometry identified199glycoproteins from male buds,175glycoproteins from famale buds and166glycoproteins from leaf buds in P. simonii x P. nigra. Comparison glycoproteins from male buds, female buds and leaf buds show41proteins were identified in male buds, female buds and leaf buds.75proteins were identified only in male buds,33proteins were identified only in famale buds,33proteins were identified only in leaf buds.255different proteins were isolated and identified in three tissuesProteins function classification showed:255glycoprotein is divided into10clusters, mainly involved in cell wall synthesis and metabolism, redox, protein degradation, signal transduction, lipid metabolism and other biological pathways. The number of the top four proteins function clustering followed by cell wall synthesis, modification and carbohydrate metabolism (33%), redox (22%), protein degradation (12%) and signal transduction (10%). We isolated and identified glycoprotein function classification mode, similar to the characteristics of the functional classification of Arabidopsis cell wall proteome, this implies that the plant cell wall protein preliminary agreement is likely to have been glycosylated and glycosylated may be cell wall protein required for normal function of the molecule.In order to evaluate glycoproteins using biological information related software analysis N-glycosylation sites and signal peptide of255glycoproteins.226glycoproteins having N-glycosylation sites, representing glycosylated protein group was89%.189glycosylated protein having a signal peptide, glycosylated protein representing74%of the group. This analysis showed that the isolation and identification of P. simonii x P. nigra flower buds and leaf buds organizations glycosylated protein with high reliability.Analysis of the subcellular localization of proteins and transmembrane domains display:83%glycoproteins involves secretory pathway,53%glycoproteins localized in cell wall,18%glycoproteins localized in cell membrane,8%glycoproteins localized in endoplasmic reticulum,6%glycoproteins localized in vacuoles,15%glycoprotein localized in other parts of cellula. Furthermore,34%glycoproteins include transmembrane domain. This result shows that we recognize glycoproteins are mainly of plant cell wall proteins.Our work is the first large-scale separation and identification of woody plants total glycoprotein proteome, the functional classification of protein glycosylation, location analysis, preliminary information displayed poplar cell wall protein glycosylation prevalent. These data for future identification of plant cell wall protein glycosylation molecular role in providing an important foundation.