Analysis of Efg1 co-purifying proteins
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)
SUBMITTER: 
Jochen Baßler
LAB HEAD: Jochen Baßler
PROVIDER: PXD036987 | Pride | 2023-11-27
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Efg1.raw | Raw | |||
| Kre33.raw | Raw | |||
| allSpectra.CID.ITMS.iso_0.apl | Other | |||
| allSpectra.CID.ITMS.iso_1.apl | Other | |||
| allSpectra.CID.ITMS.iso_10.apl | Other |
Items per page: 5 1 - 5 of 28 |
Similar Datasets
Project description:Analysis of Efg1 co-purifying proteins in comparison to Bud22 particle
2023-11-27 | PXD042897 | Pride
Project description:Analysis of Utp10 co-purifying proteins from wildtype, Efg1 depleted and Bud22 depleted background
2023-11-27 | PXD042906 | Pride
Project description:Ribosome biogenesis follows a hierarchical set of pre-ribosomal RNA (pre-RNA) folding and processing steps. The earliest, biochemically stable pre-ribosome is the 90S particle, which is assembled co-transcriptionally in the nucleolus. It is unclear how pre-rRNA, ribosomal proteins and assembly factors play together in the early stages of 90S maturation. Is has remained unclear, how the numerous snoRNAs, which guide pre-rRNA modification and folding while the nascent rRNA is flexible and hence accessible, are involved in pre-ribosomal maturation. Here, we identify the conserved C-terminus of assembly factor Krr1 as crucial for efficient release of the essential snR30. Furthermore, we show that snR30 is bound to the central domain of the 18S rRNA within a complex that contains assembly factors and ribosomal proteins. Our study shows how independent 18S domain maturation is guided by snR30 in coupling rRNA chaperoning with the delivery of ribosomal proteins.
2025-05-22 | PXD054032 | Pride
Project description:Ribosome biogenesis follows a hierarchical set of pre-ribosomal RNA (pre-RNA) folding and processing steps. The earliest, biochemically stable pre-ribosome is the 90S particle, which is assembled co-transcriptionally in the nucleolus. It is unclear how pre-rRNA, ribosomal proteins and assembly factors play together in the early stages of 90S maturation. Is has remained unclear, how the numerous snoRNAs, which guide pre-rRNA modification and folding while the nascent rRNA is flexible and hence accessible, are involved in pre-ribosomal maturation. Here, we identify the conserved C-terminus of assembly factor Krr1 as crucial for efficient release of the essential snR30. Furthermore, we show that snR30 is bound to the central domain of the 18S rRNA within a complex that contains assembly factors and ribosomal proteins. Our study shows how independent 18S domain maturation is guided by snR30 in coupling rRNA chaperoning with the delivery of ribosomal proteins.
2025-05-22 | PXD054031 | Pride
Project description:Ribosome biogenesis follows a hierarchical set of pre-ribosomal RNA (pre-RNA) folding and processing steps. The earliest, biochemically stable pre-ribosome is the 90S particle, which is assembled co-transcriptionally in the nucleolus. It is unclear how pre-rRNA, ribosomal proteins and assembly factors play together in the early stages of 90S maturation. Is has remained unclear, how the numerous snoRNAs, which guide pre-rRNA modification and folding while the nascent rRNA is flexible and hence accessible, are involved in pre-ribosomal maturation. Here, we identify the conserved C-terminus of assembly factor Krr1 as crucial for efficient release of the essential snR30. Furthermore, we show that snR30 is bound to the central domain of the 18S rRNA within a complex that contains assembly factors and ribosomal proteins. Our study shows how independent 18S domain maturation is guided by snR30 in coupling rRNA chaperoning with the delivery of ribosomal proteins.
2025-05-22 | PXD054035 | Pride
Project description:Ribosome biogenesis follows a hierarchical set of pre-ribosomal RNA (pre-RNA) folding and processing steps. The earliest, biochemically stable pre-ribosome is the 90S particle, which is assembled co-transcriptionally in the nucleolus. It is unclear how pre-rRNA, ribosomal proteins and assembly factors play together in the early stages of 90S maturation. Is has remained unclear, how the numerous snoRNAs, which guide pre-rRNA modification and folding while the nascent rRNA is flexible and hence accessible, are involved in pre-ribosomal maturation. Here, we identify the conserved C-terminus of assembly factor Krr1 as crucial for efficient release of the essential snR30. Furthermore, we show that snR30 is bound to the central domain of the 18S rRNA within a complex that contains assembly factors and ribosomal proteins. Our study shows how independent 18S domain maturation is guided by snR30 in coupling rRNA chaperoning with the delivery of ribosomal proteins.
2025-05-22 | PXD054034 | Pride
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 | PXD037619 | Pride
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
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
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