Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

ABSTRACT: The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

PROVIDER: PRJNA674317 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR12971900.fastq.gz	Fastqsanger.gz
	SRR12971901.fastq.gz	Fastqsanger.gz
	SRR12971902.fastq.gz	Fastqsanger.gz
	SRR12971899.fastq.gz	Fastqsanger.gz

Items per page:

1 - 4 of 4

Similar Datasets

The RNA helicase Dbp7 promotes domain VI compaction and stabilization of inter-domain interactions during early 60S assembly

Project description:Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center and is responsible for stabilizing interactions between the 5’ and 3’ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation.

2021-08-16 | GSE161347 | GEO

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

2021-08-18 | GSE160734 | GEO

The RNA helicase Dbp7 promotes domain VI compaction and stabilization of inter-domain interactions during early 60S assembly

Project description:The RNA helicase Dbp7 promotes domain VI compaction and stabilization of inter-domain interactions during early 60S assembly

| PRJNA677938 | ENA

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

2021-08-23 | PXD022625 | Pride

The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly

Project description:Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation. Early steps of large 60S ribosomal subunit biogenesis are not well understood. Here, the authors combine biochemical experiments with protein-RNA crosslinking and mass spectrometry to show that the RNA helicase Dbp7 is key player during early 60S ribosomal assembly. Dbp7 regulates a series of events driving compaction of domain V/VI in early pre60S ribosomal particles.

| S-EPMC8536713 | biostudies-literature

Heterochromatin rewiring and domain disruption-mediated chromatin compaction during erythropoiesis

Project description:Heterochromatin rewiring and domain disruption-mediated chromatin compaction during erythropoiesis

| PRJNA762583 | ENA

Heterochromatin rewiring and domain disruption-mediated chromatin compaction during erythropoiesis

Project description:Heterochromatin rewiring and domain disruption-mediated chromatin compaction during erythropoiesis

| PRJNA763785 | ENA

Heterochromatin rewiring and domain disruption-mediated chromatin compaction during erythropoiesis [HiChIP]

Project description:Heterochromatin rewiring and domain disruption-mediated chromatin compaction during erythropoiesis [HiChIP]

| PRJNA762586 | ENA

High-throughput RNA structure probing reveals critical folding events during early 60S ribosome assembly in yeast.

Project description:While the protein composition of various yeast 60S ribosomal subunit assembly intermediates has been studied in detail, little is known about ribosomal RNA (rRNA) structural rearrangements that take place during early 60S assembly steps. Using a high-throughput RNA structure probing method, we provide nucleotide resolution insights into rRNA structural rearrangements during nucleolar 60S assembly. Our results suggest that many rRNA-folding steps, such as folding of 5.8S rRNA, occur at a very specific stage of assembly, and propose that downstream nuclear assembly events can only continue once 5.8S folding has been completed. Our maps of nucleotide flexibility enable making predictions about the establishment of protein-rRNA interactions, providing intriguing insights into the temporal order of protein-rRNA as well as long-range inter-domain rRNA interactions. These data argue that many distant domains in the rRNA can assemble simultaneously during early 60S assembly and underscore the enormous complexity of 60S synthesis.Ribosome biogenesis is a dynamic process that involves the ordered assembly of ribosomal proteins and numerous RNA structural rearrangements. Here the authors apply ChemModSeq, a high-throughput RNA structure probing method, to quantitatively measure changes in RNA flexibility during the nucleolar stages of 60S assembly in yeast.

2017-10-04 | GSE83821 | GEO

Streptomyces cavourensis strain:60S

Project description:Streptomyces cavourensis strain:60S Genome sequencing

| PRJNA1119507 | ENA