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Acetylome analysis of Botrytis cinerea

ABSTRACT: Lysine acetylation of proteins is a dynamic and reversible post-translational modification that plays an important role in diverse cellular processes. Botrytis cinerea is the most thoroughly studied necrotrophic species due to its broad host range and huge economic impact. However, to date, little is known about the functions of lysine acetylation in this plant pathogen. In this study, we determined the lysine acetylome of B. cinerea through the combination of affinity enrichment and high-resolution LC-MS/MS analysis. Overall, 1582 lysine acetylation sites in 954 proteins were identified.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Botryotinia Fuckeliana (strain B05.10) (noble Rot Fungus) (botrytis Cinerea)

TISSUE(S): Mycelium

SUBMITTER: qianqian yang

LAB HEAD: Wenxing Liang

PROVIDER: PXD004031 | Pride | 2017-11-02

REPOSITORIES: Pride

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Publications

Proteome-wide analysis of lysine acetylation in the plant pathogen Botrytis cinerea.

Lv Binna B Yang Qianqian Q Li Delong D Liang Wenxing W Song Limin L

Scientific reports 20160706

Lysine acetylation is a dynamic and reversible post-translational modification that plays an important role in diverse cellular processes. Botrytis cinerea is the most thoroughly studied necrotrophic species due to its broad host range and huge economic impact. However, to date, little is known about the functions of lysine acetylation in this plant pathogen. In this study, we determined the lysine acetylome of B. cinerea through the combination of affinity enrichment and high-resolution LC-MS/M ...[more]

PMID: 27381557

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Global Proteomic Analysis of Lysine lactylation in The Plant Pathogen Botrytis cinerea

Project description:Lysinelactylation , a recently discovered post-translational modification, plays a key role in the regulation of diverse cellular processes. Botrytis cinerea is a destructive necrotrophic fungal pathogen distributed worldwide with broad ranging hosts. However, the functions of Lysine lactylation are unknown in B. cinerea or any other plant fungal pathogens.

2020-09-07 | PXD020746 | Pride

Proteome-wide Analysis of Lysine 2-hydroxyisobutyrylation in the Phytopathogenic Fungus Botrytis cinerea

Project description:Lysine 2-hydroxyisobutyrylation , a recently discovered post-translational modification, plays a key role in the regulation of diverse cellular processes. Botrytis cinerea is a destructive necrotrophic fungal pathogen distributed worldwide with broad ranging hosts. However, the functions of Lysine 2-hydroxyisobutyrylation are unknown in B. cinerea or any other plant fungal pathogens

2020-09-07 | PXD021059 | Pride

Global Proteomic Analysis of Lysine crotonylation in The Plant Pathogen Botrytis cinerea

Project description:Lysine crotonylation (Kcr), a recently discovered post-translational modification, plays a key role in the regulation of diverse cellular processes. Botrytis cinerea is a destructive necrotrophic fungal pathogen distributed worldwide with broad ranging hosts. However, the functions of Kcr are unknown in B. cinerea or any other plant fungal pathogens. Here, we comprehensively evaluated the crotonylation proteome of B. cinerea and identified 3967 Kcr sites in 1041 proteins, of which contained in 9 types of modification motifs. Our results show that although the crotonylation were largely conserved, different organisms contained distinct crotonylated proteins with unique functions. Bioinformatic analysis demonstrated that the majority of crotonylated proteins were distributed in cytoplasm (35%), mitochondria (26%) and nucleus (22%). The identified proteins were found to be involved in various metabolic and cellular processes, such as cytoplasmic translation and structural constituent of ribosome. Particularly, 26 crotonylated proteins participated in the pathogenicity of B. cinerea, suggesting a significant role for Kcr in this process. Protein interaction network analysis demonstrated that a mass of protein interactions are regulated by crotonylation. These data represent the ﬁrst report of the crotonylome of B. cinerea and provide a good foundation for further explorations of the role of Kcr in plant fungal pathogens.

2020-09-07 | PXD019358 | Pride

The acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens

Project description:Protein lysine acetylation, a dynamic and reversible posttranslational modification, plays a crucial role in several cellular processes including cell cycle regulation, metabolic pathways, enzymatic activities and protein interactions. Brenneria nigrifluens is the pathogen of shallow bark canker of walnut trees and can cause serious disease on walnut trees. Up to now, it is little known about the roles of lysine acetylation in the plant pathogenic bacteria. In the present study, the lysine acetylome of B. nigrifluens was determined by high-resolution LC-MS/MS analysis. In total, we identified 1,866 lysine acetylation sites distributed in 737 acetylated proteins. Bioinformatics results indicate that acetylated proteins participate in many different biological functions in B. nigrifluens. Four conserved motifs, namely, LKac, Kac*F, I*Kac and L*Kac, were identified in this bacterium. Protein interaction network analysis indicates that all kinds of interactions are modulated by protein lysine acetylation. Overall, 14 acetylated proteins are related to the virulence of B. nigrifluens.

2019-09-30 | PXD014046 | Pride

Global Proteomic Analysis of Lysine Acetylation in The Plant PathogenFusarium oxysporum

Project description:Lysine acetylation (Kac), a recently discovered post-translational modification, plays a key role in the regulation of diverse cellular processes.Fusarium oxysporum is a destructive necrotrophic fungal pathogen distributed worldwide with broad ranging hosts. However, the functions of Kac are unknown in FO. or any other plant fungal pathogens. Here, we comprehensively evaluated the acetylation proteome of FO. Our results show that although the acetylation were largely conserved, different organisms contained distinct crotonylated proteins with unique functions. Bioinformatic analysis demonstrated that the majority of crotonylated proteins were distributed in cytoplasm, mitochondria and nucleus). The identified proteins were found to be involved in various metabolic and cellular processes, such as cytoplasmic translation and structural constituent of ribosome. Protein interaction network analysis demonstrated that a mass of protein interactions are regulated by acetylation. These data represent the ﬁrst report of the crotonylome of FO. and provide a good foundation for further explorations of the role of Kac in plant fungal pathogens.

2023-07-17 | PXD043826 | Pride

Label-free Quantitative Acetylomics Revealed Toxoplasma gondii Genotype-Specific Acetylome Signatures

Project description:Distinct genotypic and pathogenicity differences exist between strains of the opportunistic protozoan Toxoplasma gondii. The label-free quantitative acetylomics approach was applied to investigate the differences in the level of acetylation between RH strain, PRU strain and PYS strain of T. gondii. The results showed that lysine acetylation in RH strain was the largest (458 acetylated proteins) among the three strains. The PYS strain had the second-largest acetylome (188 acetylated proteins), whereas lysine acetylation in PRU strain (115 acetylated proteins) was the smallest. Motif analysis revealed four, three and four motifs enriched from lysine acetylation sequences in RH strain, PRU strain and PYS strain respectively, suggesting specificity of acetyltransferases in these strains. Our analysis also identified 15 DAPs (differentially expressed acetylated proteins), 3 DAPs and 26 DAPs in RH strain vs PRU strain, PRU strain vs PYS strain and PYS strain vs RH strain, respectively. Compared with PYS strain and PRU strain, histone acetyltransferase and glycyl-tRNA synthase had higher expression levels in RH strain, reflecting genotype-specific differences in stress tolerance. These findings provide novel insight into the acetylomic profiles of major genotypes of T. gondii and provide an important resource for further analysis of the roles of the acetylated parasite proteins in the regulation of cellular functions.

2020-05-27 | PXD015031 | Pride

Bacillus subtilis acetylome and succinylome

Project description:The two major acyl-modifications on lysine residues, acetylation and succinylation, were analyzed in the gram-positive model bacterium Bacillus subtilis. To identify and quantify the changes in acetylation and succinylation in response to the carbon source, a stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomic analysis of cells grown on glucose or citrate was performed.

2015-07-02 | PXD001615 | Pride

Systematic analysis of the lysine acetylome reveals diverse functions of lysine acetylation in the oleaginous yeast Yarrowia lipolytica

Project description:Lysine acetylation of proteins, a major post-translational modification, plays a critical regulatory role in almost every aspects in both eukaryotes and prokaryotes. Yarrowia lipolytica, an oleaginous yeast, is considered as a model for bio-oil production due to its ability to accumulate a large amount of lipids. However, the function of lysine acetylation in this organism is elusive. Here, we performed a global acetylproteome analysis of Y. lipolytica ACA-DC 50109. In total, 3163 lysine acetylation sites were identified in 1428 proteins, which account for 22.1% of the total proteins in the cell. Fifteen conserved acetylation motifs were detected. The acetylated proteins participate in a wide variety of biological processes. Notably, a total of 65 enzymes involved in lipid biosynthesis were found to be acetylated. The acetylation sites are distributed in almost every type of conserved domains in the multi-enzymatic complexes of fatty acid synthetases, suggesting an important regulatory role of lysine acetylation in lipid metabolism. Moreover, protein interaction network analysis reveals that diverse interactions are modulated by protein acetylation. The provided dataset probably illuminates the crucial role of reversible acetylation in oleaginous microorganisms, and serves as an important resource for exploring the physiological role of lysine acetylation in eukaryotes.

2018-11-22 | PXD006272 | Pride

Phosphoproteome profiles of the phytopathogenic fungi Alternaria brassicicola and Botrytis cinerea

Project description:This study describes the gel-free phosphoproteomic analysis the phytopathogenic fungi Alternaria brassicicola and Botrytis cinerea grown in vitro under non-limiting conditions.

2014-06-09 | PXD000817 | Pride

Acetylome analysis of Bacillus amyloliquefaciens

Project description:Lysine acetylation is a major post-translational modification that plays an important regulatory role in almost every aspects in both eukaryotes and prokaryotes. Bacillus amyloliquefaciens, a Gram-positive bacterium, is very effective for the control of plant pathogens. Here, we conducted the first lysine acetylome in B. amyloliquefaciens through a combination of highly sensitive immune-affinity purification and high-resolution LC−MS/MS. Overall, we identified 3268 lysine acetylation sites in 1254 proteins. Acetylated proteins are associated with a variety of biological processes and a large fraction of these proteins are involved in metabolism. These data serves as an important resource for further elucidation of the physiological role of lysine acetylation in B. amyloliquefaciens.

2018-10-26 | PXD003339 | Pride

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