Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Analysis of Efg1 co-purifying proteins

ABSTRACT: Analysis of Utp10 co-purifying proteins from wildtype, Efg1 depleted and Bud22 depleted background

INSTRUMENT(S): LTQ

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

SUBMITTER: Jochen Baßler

LAB HEAD: Jochen Baßler

PROVIDER: PXD042906 | Pride | 2023-11-27

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Bud22_minus_Aux.raw	Raw
	Bud22_plus_Aux.raw	Raw
	Efg1_minus_Aux.raw	Raw
	Efg1_plus_Aux.raw	Raw
	allSpectra.HCD.FTMS.iso_0.apl	Other

Items per page:

1 - 5 of 80

Similar Datasets

Analysis of Efg1 co-purifying proteins

Project description:Analysis of Efg1 co-purifying proteins in comparison to Bud22 particle

2023-11-27 | PXD042897 | Pride

Analysis of Efg1 co-purifying proteins

Project description:Analysis of Efg1 co-purifying proteins in comparison to Kre33 particle

2023-11-27 | PXD036987 | Pride

Cms1 coordinates stepwise local 90S pre-ribosome assembly with timely snR83 release - table s1 corrected

Project description:Ribosome synthesis begins in the nucleolus with 90S pre-ribosome construction, but little is known about how the many different snoRNAs that modify the pre-rRNA are timely guided to their target sites. Here, we report a role for Cms1 in such a process. Initially, we discover CMS1 as null suppressor of a nop14 mutant impaired in Rrp12–Enp1 factor recruitment to the 90S. Further investigations detect Cms1 at the 18S rRNA 3'-major domain of an early 90S that carries H/ACA snR83, known to guide pseudouridylation at two target sites within the same subdomain. Cms1 co-precipitates with many 90S factors, but Rrp12-Enp1 encircling the 3'-major domain in the mature 90S is decreased. We suggest that Cms1 associates with the 3’-major domain during early 90S biogenesis to restrict premature Rrp12–Enp1 binding, but allows snR83 to timely perform its modification role before the next 90S assembly steps coupled with Cms1 release take place.

2023-03-11 | PXD037562 | Pride

Cms1 coordinates stepwise local 90S pre-ribosome assembly with timely snR83 release Table S2

2023-03-11 | PXD037619 | Pride

Identification of phosphorylation sites in the IGF-1 Receptor

Project description:Although Insulin-like Growth Factor (IGF-1) signaling promotes tumor growth and cancer progression, IGF-1 Receptor-targeted therapies have shown poor clinical efficacy. The mechanistic basis for this is unclear as is our understanding of what distinguishes IGF-1R signaling from the closely related Insulin receptor (IR) signaling. This study illuminates both issues. A site in the IGF-1R C-terminal tail incorporating two tyrosines that are not present in the Insulin receptor (IR) was previously shown to be essential for IGF-1-mediated cancer cell survival, migration and tumorigenic growth. Here, we establish that the Y1250/Y1251 site is autophosphorylated in a cell adhesion-dependent manner.

2020-05-15 | PXD017644 | Pride

Plant Y-chromosome degeneration is retarded by haploid purifying selection.

Project description:Plant Y-chromosome degeneration is retarded by haploid purifying selection.

| PRJNA146235 | ENA

Purifying selection acting on the sequence of highly expressed proteins in the microevolution

Project description:Constraints on the rate of protein sequence evolution have been a central question in evolutionary biology. Orthology analysis between closely related species has revealed that the evolutionary speed is constrained by the expression level, with highly expressed proteins evolving slowly. This negative correlation between expression levels and evolutionary rates (known as the E-R anticorrelation) has already been widely observed in past macroevolution between species, for example, between Escherichia coli and Salmonella. However, it remains unclear whether this seemingly general law also governs microevolution, including past and de novo, within a species. To explore the ubiquitous impact of expression level on molecular evolution in bacteria, we analysed genome sequences for 99 strains of E. coli for microevolution in nature. We also analysed genomic mutations accumulated under laboratory conditions as a model of de novo microevolution. Here, we show that the E-R anticorrelation is significant in both past microevolution and de novo evolution in E. coli. Our data also indicate that purifying selection acting on highly expressed genes contributes to the ubiquity of the E-R anticorrelation. This study confirmed ongoing purifying selection acting on highly expressed genes, and implied that expression level has a ubiquitous impact on the speed of molecular diversification evolution in bacteria.

2022-09-01 | GSE189008 | GEO

The genomic distribution of transposable elements is driven by spatially variable purifying selection

Project description:The genomic distribution of transposable elements is driven by spatially variable purifying selection

| PRJEB54573 | ENA

Purifying selection acting on the sequence of highly expressed proteins in the microevolution

Project description:Purifying selection acting on the sequence of highly expressed proteins in the microevolution

| PRJNA781148 | ENA

The RNA helicase Dbp10 coordinates assembly factor association with PTC formation during ribosome biogenesis

Project description:During ribosome biogenesis a plethora of assembly factors and essential enzymes drive the unidirectional maturation of nascent pre-ribosomal subunits. The DEAD-box RNA helicase Dbp10 is suggested to restructure pre-ribosomal rRNA of the evolving peptidyl-transferase center (PTC) on nucleolar ribosomal 60S assembly intermediates. Here, we show that point mutations within conserved catalytic helicase-core motifs of Dbp10 yield a dominant-lethal growth phenotype. Such dbp10 mutants, which stably associate with pre-60S intermediates, impair pre-60S biogenesis at a nucleolar stage prior to the release of assembly factor Rrp14 and stable integration of late nucleolar factors such as Noc3. Furthermore, the binding of the GTPase Nug1 to particles isolated directly via mutant Dbp10 bait proteins is specifically inhibited. The N-terminal domain of Nug1 interacts with Dbp10 and the methyltransferase Spb1, whose pre-60S incorporation is also reduced in absence of functional Dbp10. Our data suggest that Dbp10’s helicase activity generates a crucial framework for assembly factor docking thereby permitting the progression of pre-60S maturation

2024-05-22 | PXD046068 | 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