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...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2021-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0253325 |
| _version_ | 1818736800070369280 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-18T00:42:54Z |
| format | Article |
| id | doaj.art-54a8ecaa054a4bbf81990f5014d67a50 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-18T00:42:54Z |
| publishDate | 2021-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-54a8ecaa054a4bbf81990f5014d67a502022-12-21T21:26:50ZengPublic Library of Science (PLoS)PLoS ONE1932-62032021-01-01166e025332510.1371/journal.pone.0253325Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves.Bo FengShengdong LiZongshuai WangFang CaoZheng WangGeng LiKaichang LiuLysine 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.https://doi.org/10.1371/journal.pone.0253325 |
| spellingShingle | 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. PLoS ONE |
| title | 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_short | Systematic analysis of lysine 2-hydroxyisobutyrylation posttranslational modification in wheat leaves. |
| title_sort | systematic analysis of lysine 2 hydroxyisobutyrylation posttranslational modification in wheat leaves |
| url | https://doi.org/10.1371/journal.pone.0253325 |
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