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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Format: | Article |
Language: | English |
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Maximum Academic Press
2022-01-01
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Series: | Forestry Research |
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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. |
first_indexed | 2024-03-07T20:09:13Z |
format | Article |
id | doaj.art-b467955983bd4f3991eb38a99ba3433a |
institution | Directory Open Access Journal |
issn | 2767-3812 |
language | English |
last_indexed | 2024-03-07T20:09:13Z |
publishDate | 2022-01-01 |
publisher | Maximum Academic Press |
record_format | Article |
series | Forestry Research |
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 |
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