Dataset Information

“Overlapping pictures, proteomic study of the membrane components of signaling cascades in Botrytis cinerea controlled by phosphorylation”

ABSTRACT: The phytopathogen Botrytis cinerea is a ubiquitous fungus with a high capacity to adapt its metabolism to different hosts and environmental conditions in order to deploy a variety of virulence and pathogenicity factors and develop a successful plant infection. Here we report the first comparative phosphomembranome study of B. cinerea, aimed to analyze the membrane phosphoproteins composition of the fungus and its changes under different phenotypical conditions induced by two different carbon sources as plant based elicitors: glucose and deproteinized tomato cell wall (TCW). Proteomics analysisof membrane phosphoproteins was carried out by mass spectrometry. A total of 1115 proteins were successfully identified. Further analyses showed significant differences in the phosphomembranome composition depending on the available carbon source: 64 proteins were exclusively identified or overexpressed when the fungus was cultured with glucose as a sole carbon source, and 243 proteins were exclusively identified or overexpressed with TCW. GO and KEGG enrichment and clustering interaction analysis revealed changes in the composition of phosphomembranome with increase of autophagy in glucose conditions and protein degradation process, unfolded protein response (UPR) and ribosome biogenesis in TCW conditions.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Cell Culture, Fungal Cell

SUBMITTER: Francisco Fernández-Acero

LAB HEAD: Francisco Javier Fernández Acero

PROVIDER: PXD010961 | Pride | 2019-07-15

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	150310_S_FFJC_P_01_01_45pto.msf	Msf
	150310_S_FFJC_P_01_01_45pto.raw	Raw
	150310_S_FFJC_P_02_01_45pto.msf	Msf
	150310_S_FFJC_P_02_01_45pto.raw	Raw
	150310_S_FFJC_P_03_01_45pto.msf	Msf

Items per page:

1 - 5 of 16

Publications

Proteomic study of the membrane components of signalling cascades of Botrytis cinerea controlled by phosphorylation.

Escobar-Niño Almudena A Liñeiro Eva E Amil Francisco F Carrasco Rafael R Chiva Cristina C Fuentes Carlos C Blanco-Ulate Barbara B Cantoral Fernández Jesús M JM Sabidó Eduard E Fernández-Acero Francisco Javier FJ

Scientific reports 20190708 1

Protein phosphorylation and membrane proteins play an important role in the infection of plants by phytopathogenic fungi, given their involvement in signal transduction cascades. Botrytis cinerea is a well-studied necrotrophic fungus taken as a model organism in fungal plant pathology, given its broad host range and adverse economic impact. To elucidate relevant events during infection, several proteomics analyses have been performed in B. cinerea, but they cover only 10% of the total proteins p ...[more]

PMID: 31285484

Similar Datasets

Project description:Lysosomes represent a central degradative compartment of eukaryotes, yet little is known about biogenesis and function of this organelle in parasitic protists. Whereas the mannose-6 phosphate (M6P)-dependent system is dominant for lysosomal targeting in metazoans, oligosaccharide independent sorting was reported in other eukaryotes. In this study, we investigated the phagolysosomal proteome of the human parasite Trichomonas vaginalis, protein targeting and involvement of lysosomes in hydrolase secretion. The organelles were purified using conventional Percoll and OptiPrep density gradient centrifugation, and a novel purification protocol based on phagocytosis of lactoferrin-covered magnetic nanoparticles. The analysis resulted in the lysosomal proteome of 462 proteins, which were sorted into 21 functional classes. Hydrolases represent the largest functional class and include proteases, lipases, phosphatases, glycosidases, and other hydrolases. Identification of a large set of proteins involved in vesicular trafficking (80) and turnover of actin cytoskeleton rearrangement (29) indicate high dynamics of phagolysosomal compartment. Several lysosomal proteins including the cysteine protease TvCP2 were previously shown to be secreted. Our experiment showed that secretion of TvCP2 was strongly inhibited by chloroquine that increased intralysosomal pH and thus indicated TvCP2 secretion through lysosomes rather than the classical secretory pathway. Unexpectedly, we identified in the phagolysosomal proteome divergent homologs of M6P receptor TvMPR, although T. vaginalis lacks enzymes for M6P formation. To test whether oligosaccharides are involved in lysosomal targeting, we selected the lysosome-resident cysteine protease CLCP that possesses two glycosylation sites. Mutation of any of the sites redirected CLCP to the secretory pathway. Similarly, introduction of glycosylation sites to secreted β-amylase redirected this protein to lysosomes. Thus, unlike other parasitic protists, T. vaginalis seems to utilize glycosylation as recognition marker for lysosomal hydrolases. Whether TvMPR or other possible receptors are involved in this process and what is the precise structure of the lysosomal recognition marker need to be clarified in future studies.

Project description:The process of calcium carbonate biomineralization has arisen multiple times during metazoan evolution. In the phylum Cnidaria, biomineralization has mostly been studied in the subclass Hexacorallia (i.e. stony corals) in comparison to the subclass Octocorallia (i.e. red corals); the two diverged approximately 600 million years ago. The precious Mediterranean red coral, Corallium rubrum, is an octocorallian species, which produces two distinct high-magnesium calcite biominerals, the axial skeleton and the sclerites. In order to gain insight into the red coral biomineralization process and cnidarian biomineralization evolution, we studied the protein repertoire forming the organic matrix (OM) of its two biominerals. We combined High-Resolution Mass Spectrometry and transcriptome analysis to study the OM composition of the axial skeleton and the sclerites. We identified a total of 102 OM proteins, 52 are shared between the two red coral biominerals with scleritin being the most abundant protein in each fraction. Contrary to reef building corals, the red coral is collagen-rich (10 collagen-like proteins). Agrin-like glycoproteins and proteins with sugar-binding domains are also predominant. Twenty-seven and 23 proteins were uniquely assigned to the axial skeleton and the sclerites, respectively. Their inferred regulatory function suggests that the difference between the two biominerals rather relies on the modeling of the matrix network than on specific structural components. At least one OM component appears to have been horizontally transferred from prokaryotes early during Octocorallia evolution. Our results support the view that calcification of the red coral axial skeleton likely represents a secondary calcification of an ancestral gorgonian horny axis. In addition, the comparison with stony coral skeletomes highlighted the low proportion of similar proteins between the biomineral OMs of hexacorallian and octocorallian corals, suggesting an independent acquisition of calcification in anthozoans.