Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Ruegeria pomeroyi on R/S DHPS and L-Cys compared to glucose

ABSTRACT: This project invovles the identification of the pathways responsible for the breakdown of different Sulfur containing biomolecules including R/S DHPS and L-Cys compared to glucose

INSTRUMENT(S):

ORGANISM(S): Ruegeria Pomeroyi Dss-3

SUBMITTER: Nichollas Scott

LAB HEAD: Spencer J Williams

PROVIDER: PXD069364 | Pride | 2026-06-20

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20250902_HT-11629_SW_Rpom_L_cys_B1_20250903153921.raw	Raw
	20250902_HT-11629_SW_Rpom_L_cys_B2.raw	Raw
	20250902_HT-11629_SW_Rpom_L_cys_B3.raw	Raw
	20250902_HT-11629_SW_Rpom_L_cys_B4.raw	Raw
	20250902_HT-11629_SW_Rpom_L_cys_B5.raw	Raw

Items per page:

1 - 5 of 23

Similar Datasets

Bacteroides thetaiotaomicron OMV proteomics

Project description:Comparative proteomics of Bacteroides thetaiotaomicron samples comparing the total membrane (TM) and outer membrane vesicles (OMV) of WT B. thetaiotaomicron and delta 4364

2024-10-15 | PXD043219 | Pride

Bacteroides thetaiotaomicron OMV, TM and WC comparsion of delta BT4720, delta BT_4721, delta BT_4720_4721 and WT

Project description:Proteomic comparsion of Bacteroides thetaiotaomicron OMV, TM and WC of delta BT4720, delta BT_4721, delta BT_4720_4721 and WT

2024-02-08 | PXD043360 | Pride

Identification of levoglucosan degradation pathways in bacteria

Project description:Levoglucosan is produced in the pyrolysis of cellulose and starch, including from bushfires or the burning of biofuels, and is deposited from the atmosphere across the surface of the earth. We describe two levoglucosan degrading Paenarthrobacter spp. (Paenarthrobacter nitrojuajacolis LG01 and Paenarthrobacter histidinolovorans LG02) that were isolated by metabolic enrichment on levoglucosan as sole carbon source. Genome sequencing and proteomics analysis revealed expression of a series of gene clusters encoding known levoglucosan degrading enzymes, levoglucosan dehydrogenase (LGDH, LgdA), 3-keto-levoglucosan b-eliminase (LgdB1) and glucose 3-dehydrogenase (LgdC), along with an ABC transporter cassette and associated solute binding protein. However, no homologues of 3-ketoglucose dehydratase (LgdB2) were evident. The expressed gene clusters contained a range of putative sugar phosphate isomerase/xylose isomerases with weak similarity to LgdB2. Sequence similarity network analysis of genome neighbors revealed that homologues of LgdA, LgdB1 and LgdC are generally conserved in a range of bacteria in the phyla Firmicutes, Actinobacteria and Proteobacteria. One sugar phosphate isomerase/xylose isomerase cluster (LgdB3) was identified with limited distribution mutually exclusive with LgdB2. LgdB1, LgdB2 and LgdB3 adopt similar predicted 3D folds suggesting overlapping function in processing intermediates in LG metabolism. Our findings highlight the diversity within the LGDH pathway through which bacteria utilize levoglucosan as a nutrient source.

2023-05-10 | PXD039086 | Pride

Novel cell-to-cell interactions revealed by cryotomography of a DPANN coculture system

Project description:DPANN are a widespread and highly diverse group of archaea characterised by their small size, reduced genome, limited metabolic pathways, and symbiotic existence. DPANNs are predominantly obligate ectosymbionts that depend on their host for their survival and proliferation. Despite the recent expansion in this clade, the structural and molecular details of host recognition, host-DPANN intercellular communication, and host adaptation in response to DPANN attachment remain unknown. Here, we used electron cryotomography (cryo-ET) to reveal that the Candidatus Micrarchaeota” (ARM-1) interacts with its host through intercellular proteinaceous nanotubes. These tubes (~4.5 nm wide) originate in the host, extend all the way to the DPANN cytoplasm and act like tunnels for intercellular exchange. Combining cryo-ET and sub-tomogram averaging, we revealed the in situ architectures of host and DPANN S-layers and the structures of the nanotubes in their primed and extended states, providing mechanistic insights into substrate exchange. Additionally, we performed comparative proteomics and genomic analyses to identify host proteomic changes in response to the DPANN attachment. Our results showed striking alterations in host-proteome during symbiosis and upregulation/downregulation of key cellular pathways. Collectively, these results provided unprecedented insights into the structural basis of host-DPANN communication and deepen our understanding of the host ectosymbiotic relationships.

2024-05-28 | PXD045678 | Pride

Coxiella burnetii CBU2016 Proteomics

Project description:Proteomic analysis of Coxiella burnetii to understand the function of CBU2016

2024-10-17 | PXD047783 | Pride

Quantitative analysis of the acinetoabcter baumannii proteome in response to Diclofenac and Colistin

Project description:Quantitative analysis of the acinetoabcter baumannii proteome in response to Diclofenac and Colistin

2024-10-24 | PXD047586 | Pride

Proteomic impact of the loss of GH76 in TB

Project description:Proteomic impact of the loss of GH76 in TB by comparing WT to GH76

2024-06-04 | PXD042653 | Pride

Trigger Factor in Burkholderia pseudomallei is essential for key virulence determinants including host cell internalisation, cytotoxicity, motility and stress resistance.

Project description:Melioidosis is a potentially fatal infection caused by Burkholderia pseudomallei, a bacterium that is intrinsically resistant to many commonly used antibiotics. Therefore, the identification of new drug targets is essential for the development of new and effective therapies. This study demonstrates that the Trigger Factor protein, encoded by BPSL1402, is important for the establishment of B. pseudomallei infection and is involved in multiple facets of virulence including motility, cell cytotoxicity and resistance to stress. With reports of B. pseudomallei isolated from new regions and resistance to current treatment options, the significance of this research is the identification of a novel B. pseudomallei virulence factor that can be potentially exploited for the development of new therapeutics to treat this deadly infection.

2026-04-07 | PXD067556 | Pride

Generation of an optimized Cumate circuit toolkit for tunable protein expression during in vitro and in vivo studies of Burkholderia cenocepacia: DIA experiment cumate vs Rhamnose

Project description:Inducible gene expression systems are pivotal for dissecting bacterial physiology and virulence mechanisms. Across the Burkholderia genera, a limited range of inducible systems currently exist that show minimal impacts on the proteome and allow tight regulation. In this study, we engineer a set of cumate-inducible vectors for use in Burkholderia cenocepacia that offer minimal basal expression and the ability to control B. cenocepacia gene expression within Eukaryotic cells. Through mutagenesis-based studies of cumate circuits and the cumate regulator (CymR), we generate an optimized cumate circuit (PCymRC/CymRGV) which allows the tight and tunable control of protein expression within B. cenocepacia as assessed by fluorescent and protein O-linked glycosylation analysis. Using comparative proteomics, we demonstrate cumate induction leads to both reduced and orthogonal effects on B. cenocepacia compared to widely used rhamnose based induction systems. Leveraging the cell permeability of cumate and the generation of a CTX-based chromosomal integration vector, we show inducible control of protein expression is achievable during intracellular replication of B. cenocepacia. Finally, using the ability to control intracellular expression, we demonstrate the requirement of O-linked protein glycosylation for optimal B. cenocepacia intracellular replication. Combined, this work demonstrates that cumate inducible systems allows precise and tuneable gene expression in Burkholderia even within a host-pathogen context.

2026-05-15 | PXD070275 | Pride

Generation of an optimized Cumate circuit toolkit for tunable protein expression during in vitro and in vivo studies of Burkholderia cenocepacia: DIA experiment cumate vs Rhamnose including pBBR-EV

2026-05-07 | PXD075637 | Pride