Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Intermembrane space proteome of yeast mitochondria

ABSTRACT: Characterization of the mitochondrial IMS proteome / biological replicate 4 / SNvsTot

INSTRUMENT(S): LTQ Orbitrap Velos, instrument model

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Julia Maria Burkhart

PROVIDER: PRD000709 | Pride | 2012-10-09

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	PRIDE_Exp_Complete_Ac_24150.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_24150.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_24151.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_24151.xml.gz	Xml
	PRIDE_Exp_Complete_Ac_24152.pride.mgf.gz	Mgf

Items per page:

1 - 5 of 70

Publications

Intermembrane space proteome of yeast mitochondria.

Vögtle F-Nora FN Burkhart Julia M JM Rao Sanjana S Gerbeth Carolin C Hinrichs Jens J Martinou Jean-Claude JC Chacinska Agnieszka A Sickmann Albert A Zahedi René P RP Meisinger Chris C

Molecular & cellular proteomics : MCP 20120915 12

The intermembrane space (IMS) represents the smallest subcompartment of mitochondria. Nevertheless, it plays important roles in the transport and modification of proteins, lipids, and metal ions and in the regulation and assembly of the respiratory chain complexes. Moreover, it is involved in many redox processes and coordinates key steps in programmed cell death. A comprehensive profiling of IMS proteins has not been performed so far. We have established a method that uses the proapoptotic prot ...[more]

PMID: 22984289

Similar Datasets

Intermembrane space proteome of yeast mitochondria.

Project description:The intermembrane space (IMS) represents the smallest subcompartment of mitochondria. Nevertheless, it plays important roles in the transport and modification of proteins, lipids, and metal ions and in the regulation and assembly of the respiratory chain complexes. Moreover, it is involved in many redox processes and coordinates key steps in programmed cell death. A comprehensive profiling of IMS proteins has not been performed so far. We have established a method that uses the proapoptotic protein Bax to release IMS proteins from isolated mitochondria, and we profiled the protein composition of this compartment. Using stable isotope-labeled mitochondria from Saccharomyces cerevisiae, we were able to measure specific Bax-dependent protein release and distinguish between quantitatively released IMS proteins and the background efflux of matrix proteins. From the known 31 soluble IMS proteins, 29 proteins were reproducibly identified, corresponding to a coverage of >90%. In addition, we found 20 novel intermembrane space proteins, out of which 10 had not been localized to mitochondria before. Many of these novel IMS proteins have unknown functions or have been reported to play a role in redox regulation. We confirmed IMS localization for 15 proteins using in organello import, protease accessibility upon osmotic swelling, and Bax-release assays. Moreover, we identified two novel mitochondrial proteins, Ymr244c-a (Coa6) and Ybl107c (Mic23), as substrates of the MIA import pathway that have unusual cysteine motifs and found the protein phosphatase Ptc5 to be a novel substrate of the inner membrane protease (IMP). For Coa6 we discovered a role as a novel assembly factor of the cytochrome c oxidase complex. We present here the first and comprehensive proteome of IMS proteins of yeast mitochondria with 51 proteins in total. The IMS proteome will serve as a valuable source for further studies on the role of the IMS in cell life and death.

| S-EPMC3518125 | biostudies-literature

Distinct Stress Response to Mitochondrial Inter-membrane Space and Matrix Proteotoxic Stress are Preferentially Modulated by TOM complex and Vms1, respectively

Project description:Double-membrane-bound architecture of mitochondria is essential for its ATP synthesis function; simultaneously such structure sub-divides the organelle into inter-membrane space (IMS) and matrix. IMS and matrix are inherently different in protein folding milieu due to their contrasting oxido-reductive environments and distinctly different protein quality control (PQC) machineries. By inducing proteotoxic stress limited to IMS or matrix using varied stressor proteins, we decipher distinct cellular response to IMS and matrix stress. IMS stress leads to specific upregulation of IMS-resident chaperones and TOM complex components. In contrast, matrix stress leads to specific upregulation of matrix- chaperones and cytosolic PQC components. We report that cells respond to mitochondrial stress by an adaptive mechanism by adjourning mitochondrial respiration while upregulating glycolysis as a compensatory pathway. By systematic genetic interaction, we show that TOM complex components act as specific modulators of IMS-stress response while Vms1 preferentially modulates the matrix stress response

2024-07-09 | PXD027216 | Pride

Plasmodium falciparum palmitome

Project description:Acyl biotin exchange SILAC biological replicate 1, technical replicate 1

2012-09-24 | PRD000459 | Pride

Multi-omics approach to study the growth efficiency and amino acid metabolism in Lactococcus lactis at various specific growth rates

Project description:Biological replicate 1, technical replicate 1, SCX fraction 100 mM KH2PO4

2011-05-05 | PRD000266 | Pride

Study of the growth efficiency and amino acid metabolism in Lactococcus lactis at various specific growth rates

Project description:Biological replicate 2, technical replicate 1, SCX fraction 100 mM KH2PO4

2011-05-05 | PRD000267 | Pride

Impact of Exercise on Mitochondria in Cancer Patients.

Project description:The aim is to investigate the impact of prostate and colorectal cancer on mitochondrial quantity and quality along with muscle mass and function and whether this can be modified through the use of a home-based short-term exercise training program. The investigators aim to recruit participants awaiting curative surgery for colorectal and prostate cancer and to assess the variation in baseline mitochondrial activity between them. Participants from both cancer types will then carry out a 4 week home exercise program, this will be randomly allocated to either resistance-based or high-intensity interval training based. Participants will then be re-assessed on the day of their planned surgical procedure to assess the changes effected by the training program. The investigators hypothesize that there will be variation in mitochondrial activity linked to muscle mass across the two cancer types and that home-based exercise programs have the ability to improve mitochondrial activity along with muscle mass.

| 2352291 | ecrin-mdr-crc

Comprehensive identification of proteins from MALDI imaging

Project description:MALDI imaging mass spectrometry (MALDI IMS) is a powerful tool for the visualization of proteins in tissues and has demonstrated considerable diagnostic and prognostic value. One main challenge is that the molecular identity of such potential biomarkers mostly remains unknown. We introduce a method that removes this issue by systematically identifying the proteins embedded in the MALDI matrix using a combination of bottom-up and top-down proteomics. The analyses of ten human tissues lead to the identification of 1,400 abundant and soluble proteins constituting the set of proteins detectable by MALDI IMS including >90% of all IMS biomarkers reported in the literature. Top-down analysis of the matrix proteome identified 124 mostly N- and C-terminally fragmented proteins indicating considerable protein processing activity in tissues. This work presents a generic method and near complete list of MALDI IMS biomarkers that will become a valuable resource for the IMS community. Detailed description of the bioinformatics pipeline can be found in pipeline.txt. Briefly, different Mascot Distiller, Mascot and Scaffold versions have been used for the bottom-up and top-down data.

2013-07-03 | PXD000125 | Pride

Proteomic analysis of alpha4beta1 integrin adhesion complexes reveals alpha-subunit-dependent protein recruitment

Project description:Peptides and proteins identified for VCAM-1(D40A) control ligand affinity purification using K562-alpha4 cells (biological replicate 1)

2012-05-27 | PRD000565 | Pride

Circularized RNA sequencing of wild-type and Mrpp3 knock out mouse heart mitochondria

Project description:Here we find that circularization of RNA prior to deep sequencing enables the discovery and characterization of unprocessed mitochondrial RNAs. Using this approach we identify the most stable processing intermediates and the presence of intermediate processing products that are partially degraded and polyadenylated. Analysis of libraries constructed using RNA from mice lacking the nuclease subunit of the mitochondrial RNase P reveals the identities of stalled processing intermediates, their order of cleavage, and confirms the importance of RNase P (MRPP3) in generating mature mitochondrial RNAs. Using RNA circularization prior to library preparation should provide a generally useful approach to studying RNA processing in many different biological systems.

2017-03-23 | GSE94030 | GEO

Aortic extracellular space components

Project description:THORACIC AORTA GUANIDINE EXTRACT

2012-07-20 | PRD000269 | Pride