Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.

Lysine 2-hydroxyisobutyrylation (Khib) is a recently discovered post-translational modification (PTM) showing diverse biological functions and effects in living organisms. However, the study of Khib in plant species is still relatively limited. Wheat (Triticum aestivum L.) is a global important cere...

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Autores principales:	Bo Feng, Shengdong Li, Zongshuai Wang, Fang Cao, Zheng Wang, Geng Li, Kaichang Liu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/54a8ecaa054a4bbf81990f5014d67a50
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spelling	oai:doaj.org-article:54a8ecaa054a4bbf81990f5014d67a502021-12-02T20:10:26ZSystematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.1932-620310.1371/journal.pone.0253325https://doaj.org/article/54a8ecaa054a4bbf81990f5014d67a502021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0253325https://doaj.org/toc/1932-6203Lysine 2-hydroxyisobutyrylation (Khib) is a recently discovered post-translational modification (PTM) showing diverse biological functions and effects in living organisms. However, the study of Khib in plant species is still relatively limited. Wheat (Triticum aestivum L.) is a global important cereal plant. In this study, the systematic Khib analysis was performed in wheat leave tissues. A total of 3004 Khib sites in 1104 proteins were repeatedly identified. Structure characterization of these Khib peptides revealed 12 conserved sequence motifs. Function classification and enrichment analysis indicated these Khib proteins showed a wide function and pathway distribution, of which ribosome activity, protein biosynthesis and photosynthesis were the preferred biological processes. Subcellular location predication indicated chloroplast was the dominant subcellular compartment where Khib was distributed. There may be some crosstalks among Khib, lysine acetylation and lysine succinylation modification because some proteins and sites were modified by all these three acylations. The present study demonstrated the critical role of Khib in wheat biological and physiology, which has expanded the scope of Khib in plant species. Our study is an available resource and reference of Khib function demonstration and structure characterization in cereal plant, as well as in plant kingdom.Bo FengShengdong LiZongshuai WangFang CaoZheng WangGeng LiKaichang LiuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 6, p e0253325 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Bo Feng Shengdong Li Zongshuai Wang Fang Cao Zheng Wang Geng Li Kaichang Liu Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
description	Lysine 2-hydroxyisobutyrylation (Khib) is a recently discovered post-translational modification (PTM) showing diverse biological functions and effects in living organisms. However, the study of Khib in plant species is still relatively limited. Wheat (Triticum aestivum L.) is a global important cereal plant. In this study, the systematic Khib analysis was performed in wheat leave tissues. A total of 3004 Khib sites in 1104 proteins were repeatedly identified. Structure characterization of these Khib peptides revealed 12 conserved sequence motifs. Function classification and enrichment analysis indicated these Khib proteins showed a wide function and pathway distribution, of which ribosome activity, protein biosynthesis and photosynthesis were the preferred biological processes. Subcellular location predication indicated chloroplast was the dominant subcellular compartment where Khib was distributed. There may be some crosstalks among Khib, lysine acetylation and lysine succinylation modification because some proteins and sites were modified by all these three acylations. The present study demonstrated the critical role of Khib in wheat biological and physiology, which has expanded the scope of Khib in plant species. Our study is an available resource and reference of Khib function demonstration and structure characterization in cereal plant, as well as in plant kingdom.
format	article
author	Bo Feng Shengdong Li Zongshuai Wang Fang Cao Zheng Wang Geng Li Kaichang Liu
author_facet	Bo Feng Shengdong Li Zongshuai Wang Fang Cao Zheng Wang Geng Li Kaichang Liu
author_sort	Bo Feng
title	Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
title_short	Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
title_full	Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
title_fullStr	Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
title_full_unstemmed	Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
title_sort	systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/54a8ecaa054a4bbf81990f5014d67a50
work_keys_str_mv	AT bofeng systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves AT shengdongli systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves AT zongshuaiwang systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves AT fangcao systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves AT zhengwang systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves AT gengli systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves AT kaichangliu systematicanalysisoflysine2hydroxyisobutyrylationposttranslationalmodificationinwheatleaves
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Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.

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