Abstract
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.
Highlights
Protein post-translational modifications (PTMs), the covalent processing events that cleaving or adding a modifying group to an amino acid or more amino acids, are essential regulatory patterns of diverse biological processes and cellular events [1]
Previous studies have shown some PTMs such as Kac and Ksucc participate in various biological processes in wheat [29,30]
To uncover the role of Khib, a novel discovered PTM, in wheat physiology and biology, a systematic qualitative lysine 2-hydroxyisobutyrylome was performed in wheat leaves
Summary
Protein post-translational modifications (PTMs), the covalent processing events that cleaving or adding a modifying group to an amino acid or more amino acids, are essential regulatory patterns of diverse biological processes and cellular events [1]. Increasing new PTMs have been reported due to the development of high-resolution mass spectrometry (MS), such as acetylation (Kac), succinylation (Ksucc), propionylation, butyrylation and crotonylation etc [2,3,4]. With bioinformatics tools, their biological processes regulation and metabolic pathways adjustment roles have been illustrated to some extent [2,3,4]. More than 400 distinct PTMs have been reported in living various organisms [5].
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