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

ABSTRACT: 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.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Trypanosoma Brucei

TISSUE(S): Whole Body

SUBMITTER: Xianliang Ma

LAB HEAD: Wenxing Liang

PROVIDER: PXD020746 | Pride | 2020-09-07

REPOSITORIES: Pride

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			Action	DRS
	BC-1.raw	Raw
	BC-2.raw	Raw
	BC-3.raw	Raw
	BC-4.raw	Raw
	BC-5.raw	Raw

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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.

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Proteomic Analysis in The Plant PathogenFusarium oxysporum

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2023-07-17 | PXD043830 | 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

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

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Project description:We profiled small RNAs obtained from B. cinerea-infected tomato leaf and fruit during a time course. Examination of small RNAs from B. cinerea-treated tomato leaf and fruit tissue over a time course.

2014-03-11 | E-GEOD-45321 | biostudies-arrayexpress

Genome-wide high-throughput small RNA sequence analysis of B. cinerea-infected Arabidopsis rosette leaves

Project description:We profiled small RNAs obtained from B. cinerea-infected Arabidopsis rosette leaves at four different time points after inoculation. Examination of small RNA profiles of B. cinerea-infected Arabidopsis rosette leaves over a time course.

2014-03-11 | E-GEOD-45323 | biostudies-arrayexpress

Arabidopsis defense against Botrytis cinerea: chronology and regulation deciphered by high-resolution temporal transcriptomic analysis

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