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Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism
Lysine succinylation is a novel dynamic and evolutionarily conserved post-translational modification (PTM) that regulates various biological processes. ‘Anji Baicha’ is an albino tea variety that exhibits temperature-based variability of leaf colour and amino acid concentrations. However, the mechan...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431936/ https://www.ncbi.nlm.nih.gov/pubmed/28500349 http://dx.doi.org/10.1038/s41598-017-02128-x |
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author | Xu, Yan-Xia Shen, Chen-Jia Ma, Jian-Qiang Chen, Wei Mao, Juan Zhou, Yan-Yan Chen, Liang |
author_facet | Xu, Yan-Xia Shen, Chen-Jia Ma, Jian-Qiang Chen, Wei Mao, Juan Zhou, Yan-Yan Chen, Liang |
author_sort | Xu, Yan-Xia |
collection | PubMed |
description | Lysine succinylation is a novel dynamic and evolutionarily conserved post-translational modification (PTM) that regulates various biological processes. ‘Anji Baicha’ is an albino tea variety that exhibits temperature-based variability of leaf colour and amino acid concentrations. However, the mechanism underlying albinism in ‘Anji Baicha’ has not been investigated at the level of succinylation. Here, we identify 3530 lysine succinylation sites mapped to 2132 proteins in ‘Anji Baicha’, representing the first extensive data on the lysine succinylome in the tea plant. Eleven conserved succinylation motifs were enriched among the identified succinylated peptides. The protein-protein interaction maps were visualized using Cytoscape software. Comparison across three typical developmental stages of ‘Anji Baicha’ revealed that proteins exhibiting differential succinylation levels were primarily involved in photosynthesis, carbon fixation, biosynthesis of amino acids and porphyrin and chlorophyll metabolism, suggesting that these succinylated proteins are involved in ‘Anji Baicha’ leaf colour variability. These results not only deepen our understanding of the mechanism underlying ‘Anji Baicha’ albinism and the regulatory role of succinylation in the tea plant but also provide new insight into molecular breeding for leaf colour variety. |
format | Online Article Text |
id | pubmed-5431936 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-54319362017-05-16 Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism Xu, Yan-Xia Shen, Chen-Jia Ma, Jian-Qiang Chen, Wei Mao, Juan Zhou, Yan-Yan Chen, Liang Sci Rep Article Lysine succinylation is a novel dynamic and evolutionarily conserved post-translational modification (PTM) that regulates various biological processes. ‘Anji Baicha’ is an albino tea variety that exhibits temperature-based variability of leaf colour and amino acid concentrations. However, the mechanism underlying albinism in ‘Anji Baicha’ has not been investigated at the level of succinylation. Here, we identify 3530 lysine succinylation sites mapped to 2132 proteins in ‘Anji Baicha’, representing the first extensive data on the lysine succinylome in the tea plant. Eleven conserved succinylation motifs were enriched among the identified succinylated peptides. The protein-protein interaction maps were visualized using Cytoscape software. Comparison across three typical developmental stages of ‘Anji Baicha’ revealed that proteins exhibiting differential succinylation levels were primarily involved in photosynthesis, carbon fixation, biosynthesis of amino acids and porphyrin and chlorophyll metabolism, suggesting that these succinylated proteins are involved in ‘Anji Baicha’ leaf colour variability. These results not only deepen our understanding of the mechanism underlying ‘Anji Baicha’ albinism and the regulatory role of succinylation in the tea plant but also provide new insight into molecular breeding for leaf colour variety. Nature Publishing Group UK 2017-05-12 /pmc/articles/PMC5431936/ /pubmed/28500349 http://dx.doi.org/10.1038/s41598-017-02128-x Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Xu, Yan-Xia Shen, Chen-Jia Ma, Jian-Qiang Chen, Wei Mao, Juan Zhou, Yan-Yan Chen, Liang Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism |
title | Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism |
title_full | Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism |
title_fullStr | Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism |
title_full_unstemmed | Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism |
title_short | Quantitative Succinyl-Proteome Profiling of Camellia sinensis cv. ‘Anji Baicha’ During Periodic Albinism |
title_sort | quantitative succinyl-proteome profiling of camellia sinensis cv. ‘anji baicha’ during periodic albinism |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431936/ https://www.ncbi.nlm.nih.gov/pubmed/28500349 http://dx.doi.org/10.1038/s41598-017-02128-x |
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