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Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition
BACKGROUND: N(ε)-Acetylation of lysine residues, a frequently occurring post-translational modification, plays important functions in regulating physiology and metabolism. However, the information of global overview of protein acetylome under nitrogen-starvation/resupply in tea (Camellia sinensis) l...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6258439/ https://www.ncbi.nlm.nih.gov/pubmed/30477445 http://dx.doi.org/10.1186/s12864-018-5250-4 |
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author | Jiang, Jutang Gai, Zhongshuai Wang, Yu Fan, Kai Sun, Litao Wang, Hui Ding, Zhaotang |
author_facet | Jiang, Jutang Gai, Zhongshuai Wang, Yu Fan, Kai Sun, Litao Wang, Hui Ding, Zhaotang |
author_sort | Jiang, Jutang |
collection | PubMed |
description | BACKGROUND: N(ε)-Acetylation of lysine residues, a frequently occurring post-translational modification, plays important functions in regulating physiology and metabolism. However, the information of global overview of protein acetylome under nitrogen-starvation/resupply in tea (Camellia sinensis) leaves was limited. And the full function of lysine acetylated proteins of tea plants in nitrogen absorption and assimilation remains unclear. RESULTS: Here, we performed the global review of lysine acetylome in tea leaves under nitrogen (N)-starvation/resupply, using peptide prefractionation, immunoaffinity enrichment, and coupling with high sensitive LC-MS/MS combined with affinity purification analysis. Altogether, 2229 lysine acetylation sites on 1286 proteins were identified, of which 16 conserved motifs in E(*)K(ac)K, K(ac*)K, K(ac*)R, K(ac*)HK, K(ac*)N, K(ac*)S, K(ac*)T, K(ac*)D, were extracted from 2180 acetylated peptides. Approximately, 36.76% of the acetylated lysines were located in the regions of ordered secondary structures. The most of the identified lysine acetylation proteins were located in the chloroplast (39%) and cytoplasm (29%). The largest group of acetylated proteins consisted of many enzymes, such as ATP synthase, ribosomal proteins and malate dehydrogenase [NADP], which were related to metabolism (38%) in the biological process. These acetylated proteins were mainly enriched in three primary protein complexes of photosynthesis: photosystem I, photosystem II and the cytochrome b6/f complex. And some acetylated proteins related to glycolysis and secondary metabolite biosynthesis were increased/decreased under N-resupply. Moreover, the PPI (protein-protein interaction) analysis revealed that the diverse interactions of identified acetylated proteins mainly involved in photosynthesis and ribosome. CONCLUSION: The results suggested that lysine acetylated proteins might play regulating roles in metabolic process in tea leaves. The critical regulatory roles mainly involved in diverse aspects of metabolic processes, especially in photosynthesis, glycolysis and secondary metabolism. A lot of proteins related to the photosynthesis and glycolysis were found to be acetylated, including LHCA1, LHCA3, LHCB6, psaE, psaD, psaN, GAPDH, PEPC, ENL and petC. And some proteins related to flavonoids were also found to be acetylated, including PAL, DFR, naringenin 3-dioxygenase and CHI. The provided data may serve as important resources for exploring the physiological, biochemical, and genetic role of lysine acetylation in tea plants. Data are available via ProteomeXchange with identifier PXD008931. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12864-018-5250-4) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6258439 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-62584392018-11-29 Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition Jiang, Jutang Gai, Zhongshuai Wang, Yu Fan, Kai Sun, Litao Wang, Hui Ding, Zhaotang BMC Genomics Research Article BACKGROUND: N(ε)-Acetylation of lysine residues, a frequently occurring post-translational modification, plays important functions in regulating physiology and metabolism. However, the information of global overview of protein acetylome under nitrogen-starvation/resupply in tea (Camellia sinensis) leaves was limited. And the full function of lysine acetylated proteins of tea plants in nitrogen absorption and assimilation remains unclear. RESULTS: Here, we performed the global review of lysine acetylome in tea leaves under nitrogen (N)-starvation/resupply, using peptide prefractionation, immunoaffinity enrichment, and coupling with high sensitive LC-MS/MS combined with affinity purification analysis. Altogether, 2229 lysine acetylation sites on 1286 proteins were identified, of which 16 conserved motifs in E(*)K(ac)K, K(ac*)K, K(ac*)R, K(ac*)HK, K(ac*)N, K(ac*)S, K(ac*)T, K(ac*)D, were extracted from 2180 acetylated peptides. Approximately, 36.76% of the acetylated lysines were located in the regions of ordered secondary structures. The most of the identified lysine acetylation proteins were located in the chloroplast (39%) and cytoplasm (29%). The largest group of acetylated proteins consisted of many enzymes, such as ATP synthase, ribosomal proteins and malate dehydrogenase [NADP], which were related to metabolism (38%) in the biological process. These acetylated proteins were mainly enriched in three primary protein complexes of photosynthesis: photosystem I, photosystem II and the cytochrome b6/f complex. And some acetylated proteins related to glycolysis and secondary metabolite biosynthesis were increased/decreased under N-resupply. Moreover, the PPI (protein-protein interaction) analysis revealed that the diverse interactions of identified acetylated proteins mainly involved in photosynthesis and ribosome. CONCLUSION: The results suggested that lysine acetylated proteins might play regulating roles in metabolic process in tea leaves. The critical regulatory roles mainly involved in diverse aspects of metabolic processes, especially in photosynthesis, glycolysis and secondary metabolism. A lot of proteins related to the photosynthesis and glycolysis were found to be acetylated, including LHCA1, LHCA3, LHCB6, psaE, psaD, psaN, GAPDH, PEPC, ENL and petC. And some proteins related to flavonoids were also found to be acetylated, including PAL, DFR, naringenin 3-dioxygenase and CHI. The provided data may serve as important resources for exploring the physiological, biochemical, and genetic role of lysine acetylation in tea plants. Data are available via ProteomeXchange with identifier PXD008931. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s12864-018-5250-4) contains supplementary material, which is available to authorized users. BioMed Central 2018-11-26 /pmc/articles/PMC6258439/ /pubmed/30477445 http://dx.doi.org/10.1186/s12864-018-5250-4 Text en © The Author(s). 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Jiang, Jutang Gai, Zhongshuai Wang, Yu Fan, Kai Sun, Litao Wang, Hui Ding, Zhaotang Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
title | Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
title_full | Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
title_fullStr | Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
title_full_unstemmed | Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
title_short | Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
title_sort | comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6258439/ https://www.ncbi.nlm.nih.gov/pubmed/30477445 http://dx.doi.org/10.1186/s12864-018-5250-4 |
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