N-linked glycoproteome analysis reveals central glycosylated proteins involved in wheat early seedling growth

Quantitative N-Glycomic and N-Glycoproteomic Profiling of Peach [Prunus persica (L.) Batsch] during Fruit Ripening

“…Posttranslational modification, specifically N-glycosylation shows a vital part in the functional regulation of proteins. , Many N-glycoproteins in the plant including Arabidopsis , rice, wheat, maize, soybean, cotton, and barley were identified . Although N-glycosylation of proteins has been related to tomato ripening to a certain degree recently, N-glycoproteome in fruit including peach is still lacking and is in the initial stage. , Large-scale N-glycoproteome will promote our understanding of the specific role of N-glycosylation on an individual protein involved in fruit ripening. , In this work, an integrated N-glycomic and N-glycoproteomic approach was investigated to characterize the profile of protein N-glycosylation during peach ripening.…”

“…1,2 Many N-glycoproteins in the plant including Arabidopsis, rice, wheat, maize, soybean, cotton, and barley were identified. 35 Although N-glycosylation of proteins has been related to tomato ripening to a certain degree recently, N-glycoproteome in fruit including peach is still lacking and is in the initial stage. 18,26 Large-scale N-glycoproteome will promote our understanding of the specific role of N-glycosylation on an individual protein involved in fruit ripening.…”

Common Post-translational Modifications (PTMs) of Proteins: Analysis by Up-to-Date Analytical Techniques with an Emphasis on Barley

“…The results of their study showed that glycosylation sites throughout the cell are more likely to be located on a random coil, and the study also showed that glycosylation modification maintains the stability of the protein structure. 92 Because drought has a severe limiting effect on wheat growth and yield formation, a combination of a proteomics approach and Pro-Q Diamond gel staining was used to determine that several proteins are phosphorylated and up-regulated under drought conditions. Luo et al identified 58 wheat proteins that were phosphorylated among 112 differentially accumulated proteins in response to the water deficit.…”

“…performed the first analysis of the N -glycoproteome of wheat seedling leaves by enrichment glycosylation using the HILIC method and tandem mass spectrometric analysis with the use of an Orbitrap Q Exactive Plus hybrid quadrupole-Orbitrap mass spectrometer. The results of their study showed that glycosylation sites throughout the cell are more likely to be located on a random coil, and the study also showed that glycosylation modification maintains the stability of the protein structure . Because drought has a severe limiting effect on wheat growth and yield formation, a combination of a proteomics approach and Pro-Q Diamond gel staining was used to determine that several proteins are phosphorylated and up-regulated under drought conditions.…”