First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum

Abstract Histone crotonylation is a new lysine acylation type of post-translational modification (PTM) enriched at active gene promoters and potential enhancers in yeast and mammalian cells. However, lysine crotonylation in nonhistone proteins and plant cells has not yet been studied. In the present...

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Autores principales:	Hangjun Sun, Xiaowei Liu, Fangfang Li, Wei Li, Jing Zhang, Zhixin Xiao, Lili Shen, Ying Li, Fenglong Wang, Jinguang Yang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/33e6caba933c4e0680865062e5403467
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spelling	oai:doaj.org-article:33e6caba933c4e0680865062e54034672021-12-02T16:07:03ZFirst comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum10.1038/s41598-017-03369-62045-2322https://doaj.org/article/33e6caba933c4e0680865062e54034672017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03369-6https://doaj.org/toc/2045-2322Abstract Histone crotonylation is a new lysine acylation type of post-translational modification (PTM) enriched at active gene promoters and potential enhancers in yeast and mammalian cells. However, lysine crotonylation in nonhistone proteins and plant cells has not yet been studied. In the present study, we performed a global crotonylation proteome analysis of Nicotiana tabacum (tobacco) using high-resolution LC-MS/MS coupled with highly sensitive immune-affinity purification. A total of 2044 lysine modification sites distributed on 637 proteins were identified, representing the most abundant lysine acylation proteome reported in the plant kingdom. Similar to lysine acetylation and succinylation in plants, lysine crotonylation was related to multiple metabolism pathways, such as carbon metabolism, the citrate cycle, glycolysis, and the biosynthesis of amino acids. Importantly, 72 proteins participated in multiple processes of photosynthesis, and most of the enzymes involved in chlorophyll synthesis were modified through crotonylation. Numerous crotonylated proteins were implicated in the biosynthesis, folding, and degradation of proteins through the ubiquitin-proteasome system. Several crotonylated proteins related to chromatin organization are also discussed here. These data represent the first report of a global crotonylation proteome and provide a promising starting point for further functional research of crotonylation in nonhistone proteins.Hangjun SunXiaowei LiuFangfang LiWei LiJing ZhangZhixin XiaoLili ShenYing LiFenglong WangJinguang YangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hangjun Sun Xiaowei Liu Fangfang Li Wei Li Jing Zhang Zhixin Xiao Lili Shen Ying Li Fenglong Wang Jinguang Yang First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum
description	Abstract Histone crotonylation is a new lysine acylation type of post-translational modification (PTM) enriched at active gene promoters and potential enhancers in yeast and mammalian cells. However, lysine crotonylation in nonhistone proteins and plant cells has not yet been studied. In the present study, we performed a global crotonylation proteome analysis of Nicotiana tabacum (tobacco) using high-resolution LC-MS/MS coupled with highly sensitive immune-affinity purification. A total of 2044 lysine modification sites distributed on 637 proteins were identified, representing the most abundant lysine acylation proteome reported in the plant kingdom. Similar to lysine acetylation and succinylation in plants, lysine crotonylation was related to multiple metabolism pathways, such as carbon metabolism, the citrate cycle, glycolysis, and the biosynthesis of amino acids. Importantly, 72 proteins participated in multiple processes of photosynthesis, and most of the enzymes involved in chlorophyll synthesis were modified through crotonylation. Numerous crotonylated proteins were implicated in the biosynthesis, folding, and degradation of proteins through the ubiquitin-proteasome system. Several crotonylated proteins related to chromatin organization are also discussed here. These data represent the first report of a global crotonylation proteome and provide a promising starting point for further functional research of crotonylation in nonhistone proteins.
format	article
author	Hangjun Sun Xiaowei Liu Fangfang Li Wei Li Jing Zhang Zhixin Xiao Lili Shen Ying Li Fenglong Wang Jinguang Yang
author_facet	Hangjun Sun Xiaowei Liu Fangfang Li Wei Li Jing Zhang Zhixin Xiao Lili Shen Ying Li Fenglong Wang Jinguang Yang
author_sort	Hangjun Sun
title	First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum
title_short	First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum
title_full	First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum
title_fullStr	First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum
title_full_unstemmed	First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum
title_sort	first comprehensive proteome analysis of lysine crotonylation in seedling leaves of nicotiana tabacum
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/33e6caba933c4e0680865062e5403467
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_version_	1718384768255524864

First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum

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