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 Efg1 co-purifying proteins in comparison to Bud22 particle

INSTRUMENT(S): LTQ

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

SUBMITTER: Jochen Baßler

LAB HEAD: Jochen Baßler

PROVIDER: PXD042897 | Pride | 2023-11-27

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	143_2023_JB_Bud22.raw	Raw
	143_2023_JB_Efg1.raw	Raw
	allSpectra.HCD.FTMS.secpep.sil0_0.apl	Other
	allSpectra.HCD.FTMS.secpep.sil0_1.apl	Other
	allSpectra.HCD.FTMS.secpep.sil0_2.apl	Other

Items per page:

1 - 5 of 13

Similar Datasets

Analysis of Efg1 co-purifying proteins

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

2023-11-27 | PXD036987 | Pride

Analysis of Efg1 co-purifying proteins

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

2023-11-27 | PXD042906 | 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

Cotranslational signal independent SRP preloading during membrane targeting

Project description:Cotranslational targeting into the endoplasmic reticulum (ER) by the Signal Recognition Particle (SRP) is a key event determining polypeptide fate in eukaryotic cells. Here, we globally define the principles and mechanisms of SRP binding and ER targeting in vivo. Cotranslational targeting through SRP is the dominant route into the ER for all secretory proteins, regardless of targeting signal characteristics. Cytosolic SRP functions in a pioneer translation round that builds a membrane-resident mRNAs pool, explaining how low SRP levels suffice for the secretory load. SRP does not induce an elongation arrest; consequently, kinetic competition between targeting and translation elongation dictates which substrates are translocated post-translationally. Unexpectedly, SRP binds most secretory ribosomal complexes before targeting signals are synthesized. We show non-coding mRNA elements can promote signal-independent SRP pre-recruitment. Our study defines the complex kinetic interplay between elongation and determinants in the polypeptide and mRNA modulating SRP-substrate selection and membrane targeting in vivo. Ribosome profiling (RiboSeq) and RNA-seq of subcellular fractions of ribosomes. Soluble and membrane bound ribosomes are separated by centrifugation, and SRP-bound ribosomes are immunoprecipitated from the soluble fraction. Polysomes and monosomes are separated by sucrose gradient ultracentrifugation.

2016-08-03 | E-GEOD-74393 | biostudies-arrayexpress

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