Proteome-wide analyses reveal diverse functions of acetylation proteins in Neurospora crassa

Quantitative acetyl-proteomics, a newly identified post-translational modification, is known to regulate transcriptional activity in different organisms. Neurospora crassa is a model ascomycete fungus maintained for biochemistry and molecular biology research; however, extensive studies of the functions of its acylation proteins have yet to be performed. In this study, using LC-MS/MS qualitative proteomics strategies, we identified 1909 modification sites on 940 proteins in N. crassa and analysed the functions of these proteins using GO enrichment, KEGG pathway, and subcellular location experiments. We classified the acetylation protein involvement in diverse pathways, and protein-protein interaction (PPI) network analysis further demonstrated that these proteins participate in diverse biological processes. In summary, our study comprehensively profiles the crosstalk of modified sites, and PPI among these proteins may form a complex network with both similar and distinct regulatory mechanisms, providing improved understanding of their biological functions in N. crassa.

Automated summary

The study identified 1909 modification sites on 940 proteins in N. crassa using LC-MS/MS qualitative proteomics strategies. The functions of these proteins were analyzed using GO enrichment, KEGG pathway, and subcellular location experiments, revealing their involvement in diverse pathways and forming a complex protein-protein interaction (PPI) network with both similar and distinct regulatory mechanisms.