Lectin affinity-based glycoproteome analysis of the developing xylem in poplar

Glycosylation is a significant post-translational modification of proteins, and some glycoproteins serve as players in plant cell wall synthesis and modification. Wood is a highly developed cell wall organization, and protein glycosylation as a regulatory mechanism may be involved in wood formation....

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Main Authors: Hao Cheng, Jinwen Liu, Meiqi Zhou, Yuxiang Cheng
Format: Article
Language:English
Published: Maximum Academic Press 2022-01-01
Series:Forestry Research
Subjects:
Online Access:https://www.maxapress.com/article/doi/10.48130/FR-2022-0013
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author Hao Cheng
Jinwen Liu
Meiqi Zhou
Yuxiang Cheng
author_facet Hao Cheng
Jinwen Liu
Meiqi Zhou
Yuxiang Cheng
author_sort Hao Cheng
collection DOAJ
description Glycosylation is a significant post-translational modification of proteins, and some glycoproteins serve as players in plant cell wall synthesis and modification. Wood is a highly developed cell wall organization, and protein glycosylation as a regulatory mechanism may be involved in wood formation. Here, a lectin affinity-based glycoproteome was performed in stem developing xylem of poplar. After enrichment, trypsin digestion, LC-MS/MS analysis and peptide identification, we identified 154 glycoproteins from poplar developing xylem, which were classified into nine functional groups mainly including protein acting on carbohydrates, oxido-reductase, proteases, and protein kinases. Further, N- and/or O-glycosylation sites of the identified proteins were analyzed using bioinformatic tools, and deglycosylation experiments in the selected PtSOD and PtHAD proteins verified the reliability of the identified glycoproteins. Analysis of protein subcellular localization showed that a total of 63% of the identified glycoproteins were extracellular proteins or located in the plasma membrane. Poplar eFP and RT-qPCR data showed that a number of the genes encoding these glycoproteins such as laccase, peroxidase and cysteine protease, have highly preferential expression profiles in the developing xylem. Together with previously published research, most identified glycoproteins could be involved in wood cell wall synthesis and modification in poplar. Thus, our study provides some potential wood formation-related glycoproteins to be determined during tree stem development.
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spelling doaj.art-b467955983bd4f3991eb38a99ba3433a2024-02-28T01:55:27ZengMaximum Academic PressForestry Research2767-38122022-01-012111110.48130/FR-2022-0013FR-2022-0013Lectin affinity-based glycoproteome analysis of the developing xylem in poplarHao Cheng0Jinwen Liu1Meiqi Zhou2Yuxiang Cheng3Key Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, ChinaZhejiang Provincial Key Laboratory for Water Environment and Marine Biological Resources Protection, Wenzhou University, Wenzhou 325035, ChinaKey Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, ChinaKey Laboratory of Tree Genetics and Breeding, Northeast Forestry University, Harbin 150040, ChinaGlycosylation is a significant post-translational modification of proteins, and some glycoproteins serve as players in plant cell wall synthesis and modification. Wood is a highly developed cell wall organization, and protein glycosylation as a regulatory mechanism may be involved in wood formation. Here, a lectin affinity-based glycoproteome was performed in stem developing xylem of poplar. After enrichment, trypsin digestion, LC-MS/MS analysis and peptide identification, we identified 154 glycoproteins from poplar developing xylem, which were classified into nine functional groups mainly including protein acting on carbohydrates, oxido-reductase, proteases, and protein kinases. Further, N- and/or O-glycosylation sites of the identified proteins were analyzed using bioinformatic tools, and deglycosylation experiments in the selected PtSOD and PtHAD proteins verified the reliability of the identified glycoproteins. Analysis of protein subcellular localization showed that a total of 63% of the identified glycoproteins were extracellular proteins or located in the plasma membrane. Poplar eFP and RT-qPCR data showed that a number of the genes encoding these glycoproteins such as laccase, peroxidase and cysteine protease, have highly preferential expression profiles in the developing xylem. Together with previously published research, most identified glycoproteins could be involved in wood cell wall synthesis and modification in poplar. Thus, our study provides some potential wood formation-related glycoproteins to be determined during tree stem development.https://www.maxapress.com/article/doi/10.48130/FR-2022-0013glycoproteomexylempoplarlectinwood formation
spellingShingle Hao Cheng
Jinwen Liu
Meiqi Zhou
Yuxiang Cheng
Lectin affinity-based glycoproteome analysis of the developing xylem in poplar
Forestry Research
glycoproteome
xylem
poplar
lectin
wood formation
title Lectin affinity-based glycoproteome analysis of the developing xylem in poplar
title_full Lectin affinity-based glycoproteome analysis of the developing xylem in poplar
title_fullStr Lectin affinity-based glycoproteome analysis of the developing xylem in poplar
title_full_unstemmed Lectin affinity-based glycoproteome analysis of the developing xylem in poplar
title_short Lectin affinity-based glycoproteome analysis of the developing xylem in poplar
title_sort lectin affinity based glycoproteome analysis of the developing xylem in poplar
topic glycoproteome
xylem
poplar
lectin
wood formation
url https://www.maxapress.com/article/doi/10.48130/FR-2022-0013
work_keys_str_mv AT haocheng lectinaffinitybasedglycoproteomeanalysisofthedevelopingxyleminpoplar
AT jinwenliu lectinaffinitybasedglycoproteomeanalysisofthedevelopingxyleminpoplar
AT meiqizhou lectinaffinitybasedglycoproteomeanalysisofthedevelopingxyleminpoplar
AT yuxiangcheng lectinaffinitybasedglycoproteomeanalysisofthedevelopingxyleminpoplar