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Global Lysine Crotonylation Profiling of Mouse Liver
Author(s) -
Liu JiangFeng,
Wu SongFeng,
Liu Shu,
Sun Xin,
Wang XiaoMan,
Xu Ping,
Chen HouZao,
Yang JunTao
Publication year - 2020
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.202000049
Subject(s) - proteomics , biology , kegg , histone , biochemistry , metabolic pathway , proteome , computational biology , gene , epigenetics , lysine , genetics , gene ontology , amino acid , gene expression
Lysine crotonylation (Kcr) is a recently discovered post‐translational modification that potentially regulates multiple biological processes. With an objective to expand the available crotonylation datasets, LC‐MS/MS is performed using mouse liver samples under normal physiological conditions to obtain in vivo crotonylome. A label‐free strategy is used and 10 034 Class I (localization probabilities > 0.75) crotonylated sites are identified in 2245 proteins. The KcrE, KcrD, and EKcr motifs are significantly enriched in the crotonylated peptides. The identified crotonylated proteins are mostly enzymes and primarily located in the cytoplasm and nucleus. Functional enrichment analysis based on Gene Ontology and Kyoto Encyclopedia of Genes and Genomes shows that the crotonylated proteins are closely related to the purine‐containing compound metabolic process, ribose phosphate metabolic process, carbon metabolism pathway, ribosome pathway, and a series of metabolism‐associated biological processes. To the best of the authors' knowledge, this research provides the first report on the mouse liver crotonylome. Furthermore, it offers additional evidence that crotonylation exists in non‐histone proteins, and is likely involved in various biological processes. The mass spectrometry proteomics data have been deposited in the ProteomeXchange Consortium with the dataset identifiers PXD019145.