Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Growth of Aeromonas on Glucose and Chitin

ABSTRACT: Aeromonas are ubiquitous inhabitants of both natural and anthropogenic aquatic ecosystems. Occasionally, Aeromonas also grows in drinking water distribution systems, which is highly undesired due to the pathogenicity of some members of this genus. The growth of Aeromonas in such highly oligotrophic environments is currently poorly understood. Possible nutrient sources are biopolymers. For example, chitin is the structural component of the exoskeleton of insects, some invertebrates and the cell walls of fungi which makes it one of the most abundant carbon and nitrogen sources in nature. In this study we demonstrate the ability of two Aeromonas strains, Aeromonas bestiarum and Aeromonas rivuli to efficiently grow on chitin. The secreted proteins confirm the presence of the functional hydrolytic enzymes that enable the efficient degradation and utilization of this abundant biopolymer. Further quantitative cellular proteomic study unravels the remarkable reorganization of the Aeromonas metabolism when switching to chitin as sole carbon and nitrogen source. This proves that Aeromonas is not only chitinolytic but also a chitinotrophic microorganism.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Aeromonas Rivuli Aeromonas Bestiarum

TISSUE(S): Cell Culture

SUBMITTER: Martin Pabst

LAB HEAD: Martin Pabst

PROVIDER: PXD047459 | Pride | 2024-12-12

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	CT_16062023_Ab1_C_DDA01.raw	Raw
	CT_16062023_Ab1_C_DDA02.raw	Raw
	CT_16062023_Ab1_G_DDA01.raw	Raw
	CT_16062023_Ab1_G_DDA02.raw	Raw
	CT_16062023_Ab2_C_DDA01.raw	Raw

Items per page:

1 - 5 of 75

Similar Datasets

A multiomics study on the metabolism of Ca. Accumulibacter phosphatis

Project description:A metabolomics and whole cell lysate shotgun proteomics study was performed to investigate the glycolytic modes in Ca. Accumulibacter phosphatis.

2024-10-28 | PXD048326 | Pride

Salt stress in freshwater anaerobic methane-oxidizing archaea

Project description:Maider J. Echeveste Medrano and colleagues characterized the physiological and metabolic response of freshwater methanotrophic archaea to salt stress. The study performed metaproteomics, gene expression profiles and dedicated metabolomics to identify the pathways involved in the salt stress response and the osmolyte present in anaerobic methanotrophic archaea. Correspondence to Cornelia U. Welte c.welte@science.ru.nl

2024-07-17 | PXD048239 | Pride

Transcription profiling of Lotus japonicus grown under different nitrogen sources

Project description:Transcriptomic profiling was carried out for leaves of Lotus japonicus plants grown with different mineral nitrogen sources (NO3-, NH4+ or NH4NO3) or under conditions of biological nitrogen fixation (Nod). Nodulated plants were inoculated with Mesorhizobium loti and watered with nitrogen-free âHornumâ medium supplemented with 3 mM KCl. Plants under different nitrogen nutritions were watered with âHornumâ nutrient solution containing 10 mM KNO3 (NO3- plants) or with 10 mM NH4Cl supplemented with 3 mM KCl (NH4+ plants) or with 5 mM NH4NO3 supplemented with 3 mM KNO3 (NH4NO3 plants). After all the plants reached the size of 7 trifoils, leaf tissue was harvested. Every harvest involved at least three independent biological replicates for each treatment.

2016-05-17 | E-MTAB-4177 | biostudies-arrayexpress

CD95/Fas suppresses NF-B activation through recruitment of KPC2 in a CD95L/FasL-independent mechanism

Project description:CD95 expression is preserved in triple-negative breast cancers (TNBCs) and CD95 loss in these cells triggers the induction of a pro-inflammatory program promoting the recruitment of cytotoxic NK cells impairing tumor growth. Herein, we identify a novel interaction partner of CD95, Kip1 ubiquitination-promoting complex protein 2 (KPC2) using an unbiased proteomic approach. Independently of CD95L, CD95/KPC2 interaction contributes to the partial degradation of p105 (NFκB1) and the subsequent generation of p50 homodimers, which transcriptionally represses NF-κB-driven gene expression. Mechanistically, KPC2 interacts with the C-terminal region of CD95 and serves as an adaptor to recruit RelA (p65) and KPC1, which acts as E3 ubiquitin-protein ligase promoting the degradation of p105 into p50. Loss of CD95 in TNBC cells releases KPC2, limiting the formation of the NF-κB inhibitory homodimer complex (p50/p50), promoting NF-κB activation and the production of pro-inflammatory cytokines, that could account for the immune landscape remodeling in TNBC cells

2021-12-06 | PXD027196 | Pride

Chitin degradation machinery and secondary metabolite profiles in the marine bacterium Pseudoalteromonas rubra S4059

Project description:Genome mining of pigmented Pseudoalteromonas has revealed a large potential for production of bioactive compounds, both hydrolytic enzymes and secondary metabolites and the purpose of the present study was to explore this bioactivity potential in a potent antibiotic and enzyme producer, Pseudoalteromonas rubra strain S4059. Proteomic analyses indicated that a highly efficient chitin degradation machinery was present in the red-pigmented P. rubra S4059 when grown on chitin. Four GH18 chitinases and two GH20 hexosaminidases were significantly upregulated by chitin. GH19 chitinase which is not common in bacteria is consistently found in pigmented Pseudoalteromonas and in S4059 it was only detected when the bacterium was grown on chitin. To explore the possible role of GH19 in pigmented Pseudoalteromonas, we deleted the GH19 chitinase and compared a range of phenotypes in the mutant and wild type. Neither, the chitin degrading ability or the biofilm forming capacity was affected by GH19 deletion. In some Vibrionaceae, the secondary metabolome is significantly affected by growth on chitin as compared to simpler carbon sources. The secondary metabolites produced by S4059 and the GH19 mutant were xxx start by chitin/mannose – then the mutant. not altered by the absence of the gene, indicating that chitin utilization may not directly influence the production of secondary metabolites as has been observed in some Vibrionaceae. Metabolome analysis reveal that growth on chitin XX. In summary,

2021-03-11 | PXD023249 | Pride

Proteomic analysis chain-elongating microorganisms

Project description:The study by Allaart et al. (2023) investigates whether different environmental conditions can alter chain-elongating microbial communities to exhibit different catabolic stoichiometries. In support of the study, we provide whole-cell lysate shotgun proteomics data that compare the tested conditions. Contact: M.T.Allaart@tudelft.nl

2023-10-24 | PXD040972 | Pride

Chitin degradation by Vibrio sp 1A01

Project description:Proteomes of Vibrio sp. 1A01 exponentially growing on various carbon sources as well as on chitin. Chitin samples contain planktonic cells, particle-associated proteins and excreted proteins.

2022-05-19 | MSV000089499 | MassIVE

Transcription profiling of C. elegans exposed to several different bacterial pathogens

Project description:Transcritome study of C.elegans exposed to multiple, different bacterial pathogens. Experiments were performed in set-replicates of either 3 or 5.<br> There are 3 for samples: Aeromonas hydrophila, Enterococcus faecalis, Erwinia carotovora and Photorhabdus luminescens. <br> There are 5 for samples: Serratia marcesens and Escherichia coli (control).<br>

2008-02-06 | E-MEXP-766 | biostudies-arrayexpress

Genetic downregulation of Dnm2 as a therapeutic approach in a murine model of X-linked myotubular myopathy (Mtm1-/y)

Project description:In this study, we performed mass spectometry on tibialis anterior muscle of male mice. WT and Mtm1 deficient (Mtm1-/y) mice as well as on Dnm2+/- mice and on Mtm1-/y mice crossed with Dnm2+/- (Mtm1-/yDnm2+/-) were analyzed. A longitudinal follow up was established by analyzing all the genotypes at E18.5, 2w and 7w.

2022-10-13 | PXD021725 | Pride

Aeromonas jandaei DSM 7311 T6SS secretome - comparative proteomics

Project description:Label-free quantification comparative proteomics analysis of proteins secreted to the media by the T6SS of Aeromonas jandaei DSM 7311

2024-08-13 | PXD054809 | 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