Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea

Frontiers in Microbiology
Mingming GaoWenxing Liang

Abstract

Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. However, the extent of this PTM in non-histone proteins remains unknown. Here, we report the first proteomic survey of this modification in Botrytis cinerea, a destructive necrotrophic fungal pathogen distributed worldwide. After a global lysine lactylome analysis using LC-MS/MS, we identified 273 Kla sites in 166 proteins, of which contained in 4 types of modification motifs. Our results show that the majority of lactylated proteins were distributed in nucleus (36%), mitochondria (27%), and cytoplasm (25%). The identified proteins were found to be involved in diverse cellular processes. Most strikingly, Kla was found in 43 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. The combined data sets represent the first report of the lactylome of B. cinerea and provide a good foundation for furthe...Continue Reading

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Citations

Mar 9, 2021·Oxidative Medicine and Cellular Longevity·Jinlin LiuRui Guo
Jun 29, 2021·Frontiers in Immunology·An-Na ChenJin Yang
Jul 16, 2021·Journal of Agricultural and Food Chemistry·Xiaoxi MengShu Wang
Nov 2, 2021·Frontiers in Cell and Developmental Biology·Naiwen ZhangQijun Chen

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Datasets Mentioned

BETA
PXD020746

Methods Mentioned

BETA
acylation
acetylation
Lactylation
immunoprecipitation
ubiquitination

Software Mentioned

Cytoscape
MaxQuant
Andromeda engine
NetSurfP

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