Abstract
Lysine crotonylation is a newly discovered and reversible posttranslational modification involved in various biological processes, especially metabolism regulation. A total of 5159 lysine crotonylation sites in 2272 protein groups were identified. Twenty-seven motifs were found to be the preferred amino acid sequences for crotonylation sites. Functional annotation analyses revealed that most crotonylated proteins play important roles in metabolic processes and photosynthesis. Bioinformatics analysis suggested that lysine crotonylation preferentially targets a variety of important biological processes, including ribosome, glyoxylate and dicarboxylate metabolism, carbon fixation in photosynthetic organisms, proteasome and the TCA cycle, indicating lysine crotonylation is involved in the common mechanism of metabolic regulation. A protein interaction network analysis revealed that diverse interactions are modulated by protein crotonylation. These results suggest that lysine crotonylation is involved in a variety of biological processes. HSP70 is a crucial protein involved in protecting plant cells and tissues from thermal or abiotic stress responses, and HSP70 protein was found to be crotonylated in paper mulberry. This systematic analysis provides the first comprehensive analysis of lysine crotonylation in paper mulberry and provides important resources for further study on the regulatory mechanism and function of the lysine crotonylated proteome.
Highlights
Histone posttranslational modifications (PTMs) are playing an important role in expanding the genetic code and regulating cellular physiology [1]
These research strategy of high-resolution liquid chromatography-mass spectrometry. These findings have broadened our perception of lysine crotonylation involvement in protein findings have broadened our perception of lysine crotonylation involvement in protein regulation, and they will be instrumental for illustrations of the potential functions and regulation, and they will be instrumental for illustrations of the potential functions and regulatory metabolism of this newly identified PTM in woody plants
ToTo better understand the function ofof the substrates ofof lysine crotonylation inin paper mulberry, we classified all of the crotonylated proteins to a gene ontology (GO)
Summary
Histone posttranslational modifications (PTMs) are playing an important role in expanding the genetic code and regulating cellular physiology [1]. A study by Liu et al identified 1265 lysine crotonylation sites on 690 proteins in rice (Oryza sativa L. japonica) seedlings, and the results provide a comprehensive understanding of the biological functions of the crotonylome and new active histone modifications in transcriptional regulation in plants [15]. A large-scale analysis of lysine crotonyl in paper mulberry leaves was carried out through crotonylation enrichment technology and the qualitative proteomics carried out through crotonylation enrichment technology and the qualitative proteomics research strategy of high-resolution liquid chromatography-mass spectrometry. These research strategy of high-resolution liquid chromatography-mass spectrometry These findings have broadened our perception of lysine crotonylation involvement in protein findings have broadened our perception of lysine crotonylation involvement in protein regulation, and they will be instrumental for illustrations of the potential functions and regulation, and they will be instrumental for illustrations of the potential functions and regulatory metabolism of this newly identified PTM in woody plants.
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