Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Global Proteomic Analysis of Lysine Acetylation in The Plant PathogenFusarium oxysporum

ABSTRACT: 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.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Fusarium Oxysporum F. Sp. Ssl-2018a

TISSUE(S): Whole Body

SUBMITTER: Xianliang Ma

LAB HEAD: Wenxing Liang

PROVIDER: PXD043826 | Pride | 2023-07-17

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	QE_HFX_20190729_50cm_60min_Kac1.raw	Raw
	QE_HFX_20190729_50cm_60min_Kac2.raw	Raw
	QE_HFX_20190729_50cm_60min_Kac3.raw	Raw
	QE_HFX_20190729_50cm_60min_Kac4.raw	Raw
	QE_HFX_20190729_50cm_60min_Kac5.raw	Raw

Items per page:

1 - 5 of 7

Similar Datasets

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

Proteomic Analysis in The Plant PathogenFusarium oxysporum

Project description:Fusarium oxysporum is an worldwide economically important plant fungi pathogen that can cause vascular wilt disease on a wide variety of hosts (Williamson et al., 2007). In recent years, extensive research has been conducted to interpret transcriptional regulation of virulence genes in FO. (Weiberg et al., 2013;Brandhoff et al., 2017;Wang et al., 2017;Wang et al., 2018;Porquier et al., 2019). However, gaps in the protein level studies limited deeper understanding of molecular basis of FO. pathogenesis. In this study, we conducted the first proteome-wide analysis in FO.

2023-07-17 | PXD043830 | Pride

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

Global Proteomic Analysis of Lysine acetylation in Fusarium oxysporum

Project description:Lysine acetylation (Kac), a discovered post-translational modification, plays a key role in the regulation of diverse cellular processes. Fusarium oxysporumis a destructive necrotrophic fungal pathogen distributed worldwide with broad ranging hosts. However, the functions of Kac are unknown in Fusarium oxysporumr any other plant fungal pathogens. Here, we comprehensively evaluated the acetylation proteome ofFusarium oxysporum .

2021-09-09 | PXD020479 | 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

First proteomic analysis of lysine acetylation on extensive functions in Solenopsis invicta Buren

Project description:Lysine acetylation (Kac) plays a critical role in the regulation of a great deal of important cellular processes. However, little is known about Kac in Solenopsis invicta, which is one of the 100 most dangerous invasive species in the world. Lysine acetylome in S. invicta was evaluated for the first time in this study. Altogether, 2387 Kac sites were tested in 992 proteins. The prediction of subcellular localization indicated that most identified proteins were located in cytoplasm, mitochondria and nucleus. The enriched Kac site motifs included Kac H, Kac Y, Kac G, Kac F, Kac T, and Kac W. H, Y, F, and W were of frequent occurrence at the +1 position, whereas G, Y and T were of frequent occurrence at the –1 position. Based on cellular component, acetylated proteins were enriched in cytoplasmic part, mitochondrial matrix, and cytosolic ribosome. Furthermore, 25 pathways were detected to be significantly enriched. Interestingly, arginine and proline metabolism as well asphagosome, which were related to immunity, contained several Kac proteins. Acetylation or deacetylation of the proline and phagosome proteins may adjust the protein function, which may be why S. invicta was highly immune. As for interaction network investigation, diverse interactions were adjusted by Kac. Our study of lysine acetylome supplies abundant information for function analysis of reversible Kac in the growth and development of S. invicta and other Hymenoptera insects. Confirming the functions of Kac target proteins may be useful to design specific and effective drugs to prevent and control this dangerous invasive species.

2020-12-02 | PXD019033 | Pride

GlobaGlobal involvement of lysine crotonylation in protein modification and transcription regulation in ricel involvement of lysine crotonylation in protein modification and transcription regulation in rice

Project description:Lysine crotonylation (Kcr) is a newly discovered post-translational modification (PTM) existing in mammalian. Here, we performed a global crotonylome analysis of rice (Oryza sativa L. japonica) using high accuracy nano-LC-MS/MS in combination with crotonylated peptide enrichment. A total of 1,265 lysine crotonylation sites were identified on 690 proteins in rice seedlings. Subcellular localization analysis revealed that 51% of the crotonylated proteins identified were predicted to be associated with chloroplasts. The photosynthesis-associated proteins were also mostly enriched in total crotonylated proteins. Furthermore, to assess the relevance between histone Kcr and the genome, we performed a genomic localization analysis of histone Kcr by ChIP-seq analysis. Of the 10,923 identified peak regions, the majority (86.7%) of the enriched peaks were located in genes, especially exons. Furthermore, the degree of histone Kcr modification was positively correlated with gene expression in genic regions. Compared with other published histone modification data, the Kcr was co-located with the active histone modifications. Interestingly, histone Kcr facilitated expression of genes with existing active histone modifications. In addition, 77% of histone Kcr modifications overlapped with DNase hypersensitive sites (DHSs) in intergenic regions of the rice genome, and might mark other cis-regulatory DNA elements which are different from IPA1, a transcription activator in rice seedling. Overall, our results provide a comprehensive understanding of the biological functions of the crotonylome and new active histone modification in transcriptional regulation in plants.

2018-07-23 | PXD008716 | Pride

Large-Scale Analysis of Protein Crotonylation Reveals Its Diverse Functions in Pinellia ternate

Project description:We generated a global crotonylome analysis of the leaves in Pinellia ternata. We found 4509 crotonylated sites on 1757 proteins totally, and three specific amino acids surrounding crotonylation sites were identified in Pinellia ternata: KcrF, K***Y**Kcr and Kcr****R. Gene Ontology (GO) and KEGG pathway enrichment analyses showed that two crucial alkaloid biosynthesis related enzymes and many stress-related proteins were also highly crotonylated. Furthermore, several enzymes participate in the carbohydrate metabolism pathway, were modified also by lysine crotonylation.

2022-07-31 | PXD033142 | Pride

Large-Scale Analysis of Protein Crotonylation Reveals Its Diverse Functions in Pinellia ternate

2022-04-13 | PXD033154 | Pride

Systematic Analysis of the Lysine Crotonylome and multiple PTM analysis (acetylation, succinylation and crotonylation) in Candida albicans

Project description:LC-MS/MS was used to carry out the analysis of the crotonylome in C. albicans (Candida albicans) comprehensively in our study. Generally, 5242 specific crotonylated sites of 1584 crotonylated proteins were detected among 9038 proteins in C. albicans. The crotonylome involved in the regulation of metabolism through the bioinformatics analysis. Moreover, the crotonylated proteins related to biosynthesis and carbon metabolism were prevalence phenomenon. Moreover, a universal rule were found in crotonylated motifs: D/E were found in the position (+1, +2 or +3) and K/R were found in the position (+5 or +6) of the residue; A/E/F/G/P/W/Y were found in the -1 position and A/K/R were found in the position (-5, -6, -7 or -8) of the residue. As far as we know, crotonylated histone sites that screened in C. albicans of this study have not been reported before. Furthermore, a variety of connections in PPI (protein-protein interaction network) of ribosome, oxidative phosphorylation, nucleus and proteasome were modified by acetylation, succinylation and crotonylation. Sir2 inhibitor AK-1 was able to promote histone lysine crotonylation and non-histone lysine crotonylation.

2021-01-08 | PXD018848 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data