Dataset Information

Global profiling of protein lactylation in Caenorhabditis elegans (label-free quantitative proteomic data)

ABSTRACT: We identified 1836 Class I (locnalization probabilities > 0.75) lactylated sites in 487 proteis,This study establish the first lactylome database in Caenorhabditis elegans and provides a basis for studying the role of lactylation. In addition, it provides a evidence for the existence of lactylation of non-histones and their possible involvement in biological processes.

ORGANISM(S): Caenorhabditis Elegans

SUBMITTER: Juntao Yang

PROVIDER: PXD041277 | iProX | Thu Mar 30 00:00:00 BST 2023

REPOSITORIES: iProX

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Publications

Global profiling of protein lactylation in Caenorhabditis elegans.

Ding Tao T Yang Ye-Hong YH Wang Qiao-Chu QC Wu Yue Y Han Rong R Zhang Xu-Tong XT Kong Jie J Yang Jun-Tao JT Liu Jiang-Feng JF

Proteomics 20231017 1-2

Lactylation, as a novel posttranslational modification, is essential for studying the functions and regulation of proteins in physiological and pathological processes, as well as for gaining in-depth knowledge on the occurrence and development of many diseases, including tumors. However, few studies have examined the protein lactylation of one whole organism. Thus, we studied the lactylation of global proteins in Caenorhabditis elegans to obtain an in vivo lactylome. Using an MS-based platform, ...[more]

PMID: 37847886

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Project description:Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. Increasing evidence demonstrates that lysine lactylation plays an important regulatory role in metabolic processes in both bacterial and human cells. However, little is known about the extent and function of lysine lactylation in fungi, here investigated with the black yeast Phialophora verrucosaverrucose as a model organism. WeHere, we report the first proteomic survey of this modification in P. verrucosa. We performed a global lactylation analysis of P. verrucosa using high accuracy bottom-up nano-LC-MS/MS in combination wwith the enrichment of lactylated peptides from digested cell lysates and subsequent peptide identification. In total, 636 lactylation sites on 420 lactylated proteins were identified in this pathogen, of which contained in 26 types of modification motifs. Our results show that over 85% of lactylated proteins were distributed in cytoplasm, mitochondria, and nucleus. The identified proteins were found to be involved associated toin diverse biological processes and were significantly enriched in the melanin biosynthesis process. Most strikingly, Kla was found in 23 structural constituent proteins of ribosome, indicating an impact of Kla in protein synthesis . Moreover, 12 lactylated proteins participated in fungal pathogenicity, suggesting a potential role for Kla in this process. Protein interaction network analysis suggested that a mass of protein interactions are regulated by lactylation. Together, our findings reveal widespread roles for lysine lactylation in regulating metabolism and melanin biosynthesis in P. verrucosa. Our data provide a rich resource for functional analyses of lactylation and facilitate the dissection of metabolic networks in this pathogen. The combined data sets represent the first report of the lactylome of P. verrucosa and provide a good foundation for further explorations of Kla in clinical fungal pathogens.

Dataset Information

Global profiling of protein lactylation in Caenorhabditis elegans (label-free quantitative proteomic data)

Publications

Global profiling of protein lactylation in Caenorhabditis elegans.

Similar Datasets

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