Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control [II]

ABSTRACT: Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control [II]

PROVIDER: PRJNA471331 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR7163430.fastq.gz	Fastqsanger.gz
	SRR7163440.fastq.gz	Fastqsanger.gz
	SRR7163431.fastq.gz	Fastqsanger.gz
	SRR7163441.fastq.gz	Fastqsanger.gz
	SRR7163432.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 19

Similar Datasets

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control

Project description:Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control

| PRJNA471327 | ENA

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control [I]

Project description:Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control [I]

| PRJNA471315 | ENA

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control [II]

Project description:Ribosome-associated quality control (RQC) pathways monitor and respond to stalling of translating ribosomes. Using a newly developed technique based on in vivo UV crosslinking and mass spectrometry, we identify a C-terminal region in Hel2/Rqt1 as an RNA binding domain, with amino acids L501/K502 directly interacting with RNA. In vivo crosslinking of Hel2 revealed binding to 18S rRNA and translating mRNAs. Consistent with the 18S binding site located between mRNA entrance and exit channels, Hel2 preferentially bound mRNA both upstream and downstream of the termination codon. A C-terminal truncation that deleted L501/K502, abolished crosslinking to 18S rRNA, altered mRNA binding patterns, and reduced Hel2 function comparable to hel2∆. Asc1, also participates in RQC and ASC1 deletion impaired Hel2 18S and mRNA binding. We conclude that Hel2 is recruited or stabilized on translating 40S ribosomal subunits by interactions with 18S rRNA and Asc1. Ribosome-bound Hel2 interacts with mRNA, predominately during translation termination.

2019-01-18 | GSE114420 | GEO

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control [I]

2019-01-18 | GSE114415 | GEO

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control

Project description:This SuperSeries is composed of the SubSeries listed below.

2019-01-18 | GSE114429 | GEO

Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control

Project description:Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control

| PRJNA356322 | ENA

Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control.

Project description:Ribosome-associated quality control (RQC) pathways monitor and respond to ribosome stalling. Using in vivo UV-crosslinking and mass spectrometry, we identified a C-terminal region in Hel2/Rqt1 as an RNA binding domain. Complementary crosslinking and sequencing data for Hel2 revealed binding to 18S rRNA and translated mRNAs. Hel2 preferentially bound mRNAs upstream and downstream of the stop codon. C-terminal truncation of Hel2 abolished the major 18S crosslink and polysome association, and altered mRNA binding. HEL2 deletion caused loss of RQC and, we report here, no-go decay (NGD), with comparable effects for Hel2 truncation including the RNA-binding site. Asc1 acts upstream of Hel2 in RQC and asc1∆ impaired Hel2 binding to 18S and mRNA. In conclusion: Hel2 is recruited or stabilized on translating 40S ribosomal subunits by interactions with 18S rRNA and Asc1. This 18S interaction is required for Hel2 function in RQC and NGD. Hel2 probably interacts with mRNA during translation termination.

| S-EPMC6362110 | biostudies-literature

Ubiquitination of Stalled Ribosome Triggers Ribosome-associated Quality Control [SET2]

Project description:Translation elongation stalling has the potential to produce toxic truncated protein fragments. Translation of either non-stop mRNA or transcripts coding for poly-basic sequences induces ribosome stalling, and the arrest product is degraded by the ribosome-mediated quality control (RQC) system. During this process, the stalled ribosome is dissociated into subunits, and the polypeptide is ubiquitinated by the E3 ubiquitin ligase Listerin on the 60S large ribosomal subunit, leading to subsequent proteasomal degradation. However, it is largely unknown how the specific stalled ribosomes are recognized as aberrant to engage the RQC system. Here, we report that ubiquitination of the ribosomal protein uS10 of the 40S small ribosomal subunit, by the E3 ubiquitin ligase Hel2 (or RQC-trigger (Rqt) 1) initiates RQC. We identified a novel RQC-trigger (RQT) complex composed of the RNA helicase-family protein Slh1/Rqt2, the ubiquitin binding protein Cue3/Rqt3, and yKR023W/Rqt4 that is required for RQC. The defects in RQC of the RQT mutants correlated with sensitivity to anisomycin, which stalls ribosome at the rotated form, suggesting that RQT factors rescue ribosomes stalled by this drug. Our un-biased survey by ribosome profiling revealed that ribosomes stalled at the rotated state with specific pairs of codons at P-A sites serve as RQC substrates. Rqt1 specifically ubiquitinates these arrested ribosomes to target them to the RQT complex, allowing subsequent RQC reactions including dissociation of the stalled ribosome into subunits. Our results provide mechanistic insight into the surveillance system for aberrant proteins induced by ribosome stalling and mediated by ribosome ubiquitination.

2017-07-31 | GSE90919 | GEO

ZNF574 is a Quality Control Factor for Defective Ribosome Biogenesis Intermediates [CRISPRi_FLOW]

Project description:Eukaryotic ribosome assembly is an intricate process that involves four ribosomal RNAs, 80 ribosomal proteins, and over 200 biogenesis factors that take part in numerous interdependent steps. The complexity and essentiality of this process creates opportunities for deleterious mutations to occur, accumulate, and impact downstream cellular processes. “Dead-end” ribosome intermediates that result from biogenesis errors are rapidly degraded, affirming the existence of quality control pathway(s) that monitor ribosome assembly. However, the factors that differentiate between on-path and dead-end intermediates are unknown. We engineered a system to perturb ribosome assembly in human cells and discovered that faulty ribosomes are degraded via the ubiquitin proteasome system. We identified ZNF574 as a key component of a novel quality control pathway, which we term the Ribosome Assembly Surveillance Pathway (RASP). In an animal model, loss of ZNF574 leads to developmental defects, further emphasizing the importance of RASP in organismal health.

2025-05-30 | GSE275990 | GEO

ZNF574 is a Quality Control Factor for Defective Ribosome Biogenesis Intermediates [CRISPRi_growth]

2025-05-30 | GSE275991 | GEO