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Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense
The lysine crotonylation of histone proteins is a newly identified posttranslational modification with diversified cellular functions. However, there are few reports on lysine crotonylation of non-histone proteins in medicinal plant cells. By using high-resolution liquid chromatography–mass spectrom...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8888884/ https://www.ncbi.nlm.nih.gov/pubmed/35251091 http://dx.doi.org/10.3389/fpls.2022.822374 |
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author | Wu, Jing Meng, Xiaoxi Jiang, Weimin Wang, Zhaojian Zhang, Jing Meng, Fei Yao, Xiaoyan Ye, Mengjuan Yao, Liang Wang, Longhai Yu, Nianjun Peng, Daiyin Xing, Shihai |
author_facet | Wu, Jing Meng, Xiaoxi Jiang, Weimin Wang, Zhaojian Zhang, Jing Meng, Fei Yao, Xiaoyan Ye, Mengjuan Yao, Liang Wang, Longhai Yu, Nianjun Peng, Daiyin Xing, Shihai |
author_sort | Wu, Jing |
collection | PubMed |
description | The lysine crotonylation of histone proteins is a newly identified posttranslational modification with diversified cellular functions. However, there are few reports on lysine crotonylation of non-histone proteins in medicinal plant cells. By using high-resolution liquid chromatography–mass spectrometry (LC-MS) coupled with highly sensitive-specific immune-affinity antibody analysis, a whole crotonylation proteome analysis of Dendrobium huoshanense was performed. In total, 1,591 proteins with 4,726 lysine crotonylation sites were identified; among them, 11 conserved motifs were identified. Bioinformatic analyses linked crotonylated proteins to the drought stress response and multiple metabolic pathways, including secondary metabolite biosynthesis, transport and catabolism, energy production and conversion, carbohydrate transport and metabolism, translation, and ribosomal structure and biogenesis. This study contributes toward understanding the regulatory mechanism of polysaccharide biosynthesis at the crotonylation level even under abiotic stress. |
format | Online Article Text |
id | pubmed-8888884 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-88888842022-03-03 Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense Wu, Jing Meng, Xiaoxi Jiang, Weimin Wang, Zhaojian Zhang, Jing Meng, Fei Yao, Xiaoyan Ye, Mengjuan Yao, Liang Wang, Longhai Yu, Nianjun Peng, Daiyin Xing, Shihai Front Plant Sci Plant Science The lysine crotonylation of histone proteins is a newly identified posttranslational modification with diversified cellular functions. However, there are few reports on lysine crotonylation of non-histone proteins in medicinal plant cells. By using high-resolution liquid chromatography–mass spectrometry (LC-MS) coupled with highly sensitive-specific immune-affinity antibody analysis, a whole crotonylation proteome analysis of Dendrobium huoshanense was performed. In total, 1,591 proteins with 4,726 lysine crotonylation sites were identified; among them, 11 conserved motifs were identified. Bioinformatic analyses linked crotonylated proteins to the drought stress response and multiple metabolic pathways, including secondary metabolite biosynthesis, transport and catabolism, energy production and conversion, carbohydrate transport and metabolism, translation, and ribosomal structure and biogenesis. This study contributes toward understanding the regulatory mechanism of polysaccharide biosynthesis at the crotonylation level even under abiotic stress. Frontiers Media S.A. 2022-02-16 /pmc/articles/PMC8888884/ /pubmed/35251091 http://dx.doi.org/10.3389/fpls.2022.822374 Text en Copyright © 2022 Wu, Meng, Jiang, Wang, Zhang, Meng, Yao, Ye, Yao, Wang, Yu, Peng and Xing. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Wu, Jing Meng, Xiaoxi Jiang, Weimin Wang, Zhaojian Zhang, Jing Meng, Fei Yao, Xiaoyan Ye, Mengjuan Yao, Liang Wang, Longhai Yu, Nianjun Peng, Daiyin Xing, Shihai Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense |
title | Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense |
title_full | Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense |
title_fullStr | Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense |
title_full_unstemmed | Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense |
title_short | Qualitative Proteome-Wide Analysis Reveals the Diverse Functions of Lysine Crotonylation in Dendrobium huoshanense |
title_sort | qualitative proteome-wide analysis reveals the diverse functions of lysine crotonylation in dendrobium huoshanense |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8888884/ https://www.ncbi.nlm.nih.gov/pubmed/35251091 http://dx.doi.org/10.3389/fpls.2022.822374 |
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