In-depth mapping of the seed phosphoproteome and N-glycoproteome of Tartary buckwheat (Fagopyrum tataricum) using off-line high pH RPLC fractionation and nLC-MS/MS

被引:10
作者
Geng, Fang [1 ]
Liu, Xin [1 ]
Wang, Jinqiu [1 ]
He, Ruilin [1 ]
Zhao, Jianglin [1 ]
Xiang, Dabing [1 ]
Zou, Liang [1 ]
Peng, Lianxin [1 ]
Zhao, Gang [1 ]
机构
[1] Chengdu Univ, Key Lab Coarse Cereal Proc, Minist Agr & Rural Affairs, Coll Pharm & Biol Engn, 2025 Chengluo Ave, Chengdu 610106, Sichuan, Peoples R China
基金
中国国家自然科学基金;
关键词
Tartary buckwheat; Phosphoproteome; Glycoproteome; ANALYSIS REVEALS; PHOSPHORYLATION MOTIFS; PROTEOMIC ANALYSIS; ARABIDOPSIS; IDENTIFICATION; PROTEINS; SATIVA; STRESS; LEAVES; PLANTS;
D O I
10.1016/j.ijbiomac.2019.07.026
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The seed of Tartary buckwheat (Fagopyrum tataricum) is rich in nutrients and functional ingredients and is recommended as a healthy cereal food. The total proteins of Tartary buckwheat seed (TBS) were extracted and digested; then, the phosphopeptides and glycopeptides were separately enriched and identified by nano liquid chromatography/tandem mass spectrometry. A total of 2613 phosphorylation sites from 1670 phosphoproteins and 404 N-glycosylation sites from 285 N-glycoproteins were identified in TBS. Function and pathway analyses showed that TBS phosphoproteins were significantly enriched in transport, energy metabolism, amino acids bio-synthesis/metabolism, and signaling and TBS N-glycoproteins were significantly enriched in modification regulation. The present study reports the first profiles of the phosphoproteome and N-glycoproteome of TBS and provides important post-translational modifications information on the proteins in TBS. The results of this study will aid the understanding of the underlying mechanism of the germination of TBS during cultivation and edible quality changes during storage and processing. (C) 2019 Elsevier B.V. All rights reserved.
引用
收藏
页码:688 / 696
页数:9
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