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Proteome-wide Analysis of Lysine 2-hydroxyisobutyrylation in Developing Rice (Oryza sativa) Seeds

文献类型： 外文期刊

作者： Meng, Xiaoxi 1 ; Xing, Shihai 1 ; Perez, Loida M. 1 ; Peng, Xiaojun 2 ; Zhao, Qingyong 3 ; Redoa, Edilberto D. 4 ; Wan 1 ;

作者机构： 1.Mississippi State Univ, Dept Biochem Mol Biol Entomol & Plant Pathol, Starkville, MS 39762 USA

2.Jingjie PTM Biolab Co Ltd, Dept Bioinformat, Hangzhou 310018, Zhejiang, Peoples R China

3.Jiangsu Acad Agr Sci, Inst Crop Sci, Nanjing 210014, Jiangsu, Peoples R China

4.Delta Res & Extens Ctr, POB 197, Stoneville, MS 38776 USA

5.Anhui Acad Chinese Med, Inst Tradit Chinese Med Resources Protect & Dev, Hefei 230000, Anhui, Peoples R China

期刊名称：SCIENTIFIC REPORTS （ 影响因子：4.379； 五年影响因子：5.133 ）

ISSN： 2045-2322

年卷期： 2017 年 7 卷

页码：

收录情况： SCI

摘要： Lysine 2-hydroxyisobutyrylation is a recently identified protein post-translational modification that is known to affect the association between histone and DNA. However, non-histone protein lysine 2-hydroxyisobutyrylation remains largely unexplored. Utilizing antibody-based affinity enrichment and nano-HPLC/MS/MS analyses of 2-hydroxyisobutyrylation peptides, we efficaciously identified 9,916 2-hydroxyisobutyryl lysine sites on 2,512 proteins in developing rice seeds, representing the first lysine 2-hydroxyisobutyrylome dataset in plants. Functional annotation analyses indicated that a wide variety of vital biological processes were preferably targeted by lysine 2-hydroxyisobutyrylation, including glycolysis/gluconeogenesis, TCA cycle, starch biosynthesis, lipid metabolism, protein biosynthesis and processing. Our finding showed that 2-hydroxyisobutyrylated histone sites were conserved across plants, human, and mouse. A number of 2-hydroxyisobutyryl sites were shared with other lysine acylations in both histone and non-histone proteins. Comprehensive analysis of the lysine 2-hydroxyisobutyrylation sites illustrated that the modification sites were highly sequence specific with distinct motifs, and they had less surface accessibility than other lysine residues in the protein. Overall, our study provides the first systematic analysis of lysine 2-hydroxyisobutyrylation proteome in plants, and it serves as an important resource for future investigations of the regulatory mechanisms and functions of lysine 2-hydroxyisobutyrylation.

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