Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Yeast Elongator Complex Elp1-6

ABSTRACT: Elongator complex Elp1-6 purified from Saccharomyces cerevisiae was analysed by crosslinking mass spectrometry.

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

SUBMITTER: Juri Rappsilber

PROVIDER: PXD038060 | JPOST Repository | Thu Nov 24 00:00:00 GMT 2022

REPOSITORIES: jPOST

ACCESS DATA

THIS DATASET HAS BEEN DELETED

Json Xml

Similar Datasets

Chip-chip from budding yeast cells with Set3 complex

Project description:Chromatin immunoprecipitation of Set3 complex applied with tilling array chip ( ChIP on chip of either Set3-TAP or Snt1-TAP) analysis demonstrated that the genome-wide localization of Set3 complex in Saccharomyces cerevisiae

2014-12-31 | GSE57916 | GEO

Crosslinking-MS analysis of Saccharomyces cerevisiae cohesin with or without binding of Mrc1

Project description:Crosslinking-MS analysis of Saccharomyces cerevisiae cohesin complex with or without binding with Mrc1.

2023-05-04 | PXD039609 | JPOST Repository

Identification of a host protein interacting with Tomato spotted wilt virus ribonucleoproteins from Nicotiana benthamiana and yeast.

Project description:Viruses are obligate intracellular pathogens that depend on host factors to complete their infection cycle. Very little is known of which plant factors are required for successful Tomato spotted wilt orthotospovirus (TSWV) infection. The viral ribonucleoprotein (RNP) fraction from TSWV infected Nicotiana benthamiana plants was purified and its protein composition was analysed by proteomics by mass spectrometry to identify host proteins that co-purify with viral RNPs. Related, we expressed a TSWV replicon system in a non-host system, Bakers’ yeast (Saccharomyces cerevisiae), and purified as well the RNP fraction from yeast. Comparative proteomics was used to find common enriched proteins observed in both yeast and plant RNP fractions.

2021-11-10 | PXD026246 | Pride

Expression-profiling of the Mediator transcription complex

Project description:Proteins from within the Saccharomyces cerevisiae Mediator transcription complex were knocked out and compared against wild type yeast using two-color oligo arrays.

2005-08-15 | E-UMCU-20 | biostudies-arrayexpress

Cross-linking/mass spectrometry analysis of the AOC complex

Project description:As a part of a study on how kinetochors are assembled at the centromeres of the chromosomes, cross-linking/mass spectrometry has been applied to investigate interactions between Okp1/ Ame1 heterodimer, which is part of the COMA complex, and CENP-A from Saccharomyces cerevisiae.

2018-10-30 | PXD009648 | Pride

Single-copy locus proteomics of early- and late-firing DNA replication origins identifies a role of Ask1/DASH complex in replication timing control

Project description:The chromatin at origins of replication is thought to influence DNA replication initiation in eukaryotic genomes. However, it remains unclear how the chromatin composition controls the firing of early-efficient (EE) or late-inefficient (LI) origins. Here, we used site-specific recombination and single-locus chromatin isolation to purify EE and LI replication origins in Saccharomyces cerevisiae. Using mass spectrometry, we define the histone modification landscape and identify the protein composition of native chromatin regions surrounding the EE and LI replication start sites. In addition to the known origin interactors, we find novel origin-associated factors, such as the kinetochore-associated Ask1/DASH complex. Strikingly, we show that Ask1 regulates the replication timing control of specific origins in yeast. Thus, our unbiased approach identifies functionally-relevant proteomes at single-copy loci and would be widely applicable to provide an in-depth quantitative characterization of histone modification and protein interaction networks of chromatin at any genomic locus of interest.

2023-01-01 | GSE212974 | GEO

Paf1 complex subunit Rtf1 stimulates H2B ubiquitylation by interacting with the highly conserved N-terminal helix of Rad6

Project description:Histone modifications coupled to transcription elongation play important roles in regulating the accuracy and efficiency of gene expression. The mono-ubiquitylation of a conserved lysine in H2B (K123 in Saccharomyces cerevisiae and K120 in humans) occurs co-transcriptionally and is required for initiating a histone modification cascade on active genes. H2BK123 ubiquitylation (H2BK123ub) requires the RNA polymerase II (RNAPII)-associated Paf1 transcription elongation complex (Paf1C). Through its Histone Modification Domain (HMD), the Rtf1 subunit of Paf1C directly interacts with the ubiquitin conjugase Rad6, leading to the stimulation of H2BK123ub in vivo and in vitro. To understand the molecular mechanisms that specifically target Rad6 to its histone substrate, we identified the site of interaction for the HMD on Rad6. Using in vitro crosslinking followed by mass spectrometry, we localized the primary contact surface for the HMD to the highly conserved N-terminal helix of Rad6. Using a combination of genetic and biochemical experiments, we identified separation-of-function mutations in RAD6 that greatly impair H2BK123 ubiquitylation but not other Rad6 functions. Finally, by employing RNA-sequencing as a sensitive approach for comparing mutant phenotypes, we show that mutating either side of the proposed Rad6-HMD interface yields strikingly similar transcriptome profiles that extensively overlap with those of a mutant that lacks the site of ubiquitylation in H2B. Our results fit a model in which a specific interface between a transcription elongation factor and a ubiquitin conjugase guides substrate selection toward a highly conserved chromatin target during active gene expression.

2023-05-01 | GSE218023 | GEO

yeast wt-matA pool

Project description:Contains a collection of wildtype matA Saccharomyces cerevisiae strains for estimating the biological variation.

2012-11-14 | GSE42240 | GEO

An Mtw1 C-terminal motif is crucial for cooperative outer kinetochore assembly in budding yeast

Project description:We employed chemical crosslinking and mass spectrometry on KMN complexes isolated from S. cerevisiae.

2020-09-30 | PXD011774 | Pride

Yeast Nuclear Large Scale Cross-linking MS

Project description:Here, we apply large scale cross-linking mass spectrometry to profile the interactome of isolated and intact Saccharomyces cerevisiae nuclei. Two independent biological replicates (nuclei isolated from different cultures) were performed.

2020-03-12 | PXD014584 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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