Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Complexome Profiling of the thylakoid proteome from Viscum album

ABSTRACT: Viscum album is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). We here present an investigation of the V. album energy metabolism taking place in the chloroplasts. Thylakoids were purified from young V. album leaves and membrane bound protein complexes characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Viscum Album

TISSUE(S): Leaf

SUBMITTER: Lucie Schröder

LAB HEAD: Hans-Peter Braun

PROVIDER: PXD035825 | Pride | 2022-08-18

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	L51.raw	Raw
	L52.raw	Raw
	L53.raw	Raw
	L54.raw	Raw
	L55.raw	Raw

Items per page:

1 - 5 of 46

Similar Datasets

Complexome Profiling of the thylakoid proteome from Arabidopsis thaliana

Project description:We here present an investigation of the Arabidopsis thaliana energy metabolism taking place in the chloroplasts. Thylakoids were purified from Arabidopsis thaliana leaves and membrane bound protein complexes characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics.

2022-08-18 | PXD035871 | Pride

Complexome Profiling of the mitochondrial proteome from Viscum album

Project description:Viscum album is known for its special mode of cellular respiration. It lacks the mitochondrial NADH dehydrogenase complex (complex I of the respiratory chain) and has restricted capacities to generate mitochondrial adenosine triphosphate (ATP). We here present an investigation of the V. album energy metabolism taking place in mitochondria. Mitochondria were purified from young V. album leaves and membrane bound protein complexes characterized by Blue native polyacrylamide gel electrophoresis as well as by the complexome profiling approach. Proteins were systematically identified by label-free quantitative shotgun proteomics.

2023-10-24 | PXD041061 | Pride

Complexome Profiling of the mitochondrial proteome from Viscum album

Project description:Recent genomic studies revealed that mitochondria from mistletoe species appear to lack a major amount of genes, indicating a possible loss of the NADH ubiquinone oxidoreductase (complex I) which forms an essential part of the mitochondrial Oxidative Phosphorylation System (OXPHOS). This dataset is used for profiling of the mitochondrial complexome from European mistletoe, Viscum album and gives biochemical evidence for a lack of complex I as well as a unique composition of OXPHOS in Viscum album.

2018-04-23 | PXD008974 | Pride

PPR proteins in Arabidopsis mitoribosomes

Project description:Investigation of the protein composition of mitoribosomal subunits in Arabidopsis thaliana by complexome profiling

2019-04-30 | PXD011088 | Pride

Complexome profiling of mitochondria to study NDUFAF1 mediated complex I assembly in Yarrowia lipolytica

Project description:The aerobic yeast Yarrowia lipolytica is an established model organism to study mitochondrial protein complexes. Here we performed a complexome analysis of intact mitochondria to study the function of NDUFAF1 in the assembly of respiratory complex I. In the ndufaf1 deletion strain the PD module of the membrane arm accumulated but mature complex I was virtually absent.

2022-12-21 | PXD033522 | Pride

The biochemical basis of mitochondrial dysfunction in Zellweger Spectrum Disorder

Project description:We identified that peroxins were still expressed in Zellweger Spectrum Disorder (ZSD) and a subset of them accumulated on the mitochondrial membrane, which resulted in gross mitochondrial abnormalities and impaired mitochondrial metabolic function. In this complexome analysis we detected several peroxins in the mitochondrial fraction in the absence of functional peroxisomes and that this accumulation is exacerbated by the loss of the mitochondrial extractase Msp1. In addition, we observed that specific peroxisomal matrix proteins localize to the mitochondria, which suggest that a functional peroxisomal docking and import complex assembles on the mitochondria in the absence of peroxisomes.

2021-06-25 | PXD024625 | Pride

Quantification of mitochondrial complexes in DNAJC30 deficient HEK cells

Project description:We identified DNAJC30 as a key protein in the maintenance of functional NADH:ubiquinone oxidoreductase (complex I). Here we isolated and quantified complexes of the oxidative phosphorylation system (OXPHOS) in DNAJC30 deficient HEK cells.

2021-09-09 | PXD022339 | Pride

Protein turnover rates within mitochondrial complexes in mitochondrial disease patients and in a DNAJC30 knock-out cell line

Project description:We identified DNAJC30 as a key protein in the maintenance of functional NADH:ubiquinone oxidoreductase (complex I). To determine the turnover rates of modules in complex I and other mitochondrial complexes, we pulsed both patient and control fibroblast cell lines and a DNAJC30 knock-out HEK and control HEK cell line over 12 hours with heavy amino acids (PulseSILAC) followed by mass spectrometry.

2021-09-09 | PXD021548 | Pride

Complexome profiling of mitochondrial protein complexes from patients with mutation in NDUFAF8 gene

Project description:NDUFAF8 is an assembly factor of the NADH:ubiquinone oxidoreductase (complex I). Here we used complexome profiling the functional consequences of NDUFAF8 mutations in patient fibroblasts.

2020-03-05 | PXD015749 | Pride

Complexome profiling of brain mitochondria from WT and ClpP-/- mice

Project description:Mutations in the gene for the mitochondrial matrix protease CLPP can cause human Perrault syndrome, which is characterized by male and female infertility, progressive sensorineural deafness, ataxia and leukoencephalopathy. This gene encodes a peptidase that is conserved since bacteria and localizes to mitochondrial matrix in eukaryotes. To assess the assembly and stability of mitochondrial complexes brain tissue of WT and ClpP-/- mice was dissected and enriched mitochondrial fraction was used for complexome profiling.

2024-01-17 | PXD036901 | 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