Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT

ABSTRACT: Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT

PROVIDER: PRJNA472972 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR7214390.fastq.gz	Fastqsanger.gz
	SRR7214400.fastq.gz	Fastqsanger.gz
	SRR7214410.fastq.gz	Fastqsanger.gz
	SRR7214420.fastq.gz	Fastqsanger.gz
	SRR7214391.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 44

Similar Datasets

Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT

Project description:Folding newly synthesized proteins relies on the ribosome intricately coordinating mRNA translation with a network of ribosome-associated machinery. The principles that drive the coordination of this diverse machinery remain poorly understood. Here, we use selective ribosome profiling to determine how the essential chaperonin TRiC/CCT and the Hsp70 Ssb are recruited to ribosome-nascent chain complexes to mediate cotranslational protein folding. Whereas substrate localization and nascent chain sequence are the major determinants of cotranslational recruitment of Ssb, we found that temporal and structural elements drive TRiC engagement. For both chaperones, however, local slowdowns in translation enhance chaperone enrichment. This work helps define the principles that dictate the coordinated activity of ribosome-associated factors to perform their critical role in maintaining a properly folded nascent proteome.

2019-08-22 | GSE114882 | GEO

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]

Project description:The molecular chaperonin TRiC/CCT is a large hetero-oligomeric structure that serves an essential role in eukaryotic cells by minimally supporting protein homeostasis including the folding of nascent polypeptides and the assembly/disassembly of protein complexes. TRiC/CCT is typically considered a strict cytosolic machine. Here, we investigated the influence of TRiC/CCT on nuclear features including epigenetic marks, chromatin accessibility, and transcription. Despite being linked to several chromatin modifiers, our work indicates TRiC/CCT does not have a sustained role with these factors. TRiC/CCT did actively contribute to transcription. Inactivation of TRiC/CCT resulted in a significant increase in the production of RNA leading to an accumulation of noncoding transcripts. Our data support a direct role for TRiC/CCT with RNA polymerase II as the chaperonin modulated nascent RNA production both in vivo and in vitro. Overall, our studies reveal a new avenue by which TRiC/CCT contributes to cell homeostasis by regulating the activity of nuclear RNA polymerase II.

2025-09-01 | GSE274455 | GEO

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]

2025-09-01 | GSE274454 | GEO

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]

2025-09-01 | GSE274453 | GEO

Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT.

Project description:Cotranslational protein folding requires assistance from elaborate ribosome-associated chaperone networks. It remains unclear how the changing information in a growing nascent polypeptide dictates the recruitment of functionally distinct chaperones. Here, we used ribosome profiling to define the principles governing the cotranslational action of the chaperones TRiC/CCT and Hsp70/Ssb. We show that these chaperones are sequentially recruited to specific sites within domain-encoding regions of select nascent polypeptides. Hsp70 associates first, binding select sites throughout domains, whereas TRiC associates later, upon the emergence of nearly complete domains that expose an unprotected hydrophobic surface. This suggests that transient topological properties of nascent folding intermediates drive sequential chaperone association. Moreover, cotranslational recruitment of both TRiC and Hsp70 correlated with translation elongation slowdowns. We propose that the temporal modulation of the nascent chain structural landscape is coordinated with local elongation rates to regulate the hierarchical action of Hsp70 and TRiC for cotranslational folding.

| S-EPMC6953483 | biostudies-literature

Folding of beta-tubulin by the chaperonin TRiC/CCT studied by chemical cross-linking and mass spectrometry

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the folding of the client protein, beta-tubulin, by the chaperonin TRiC/CCT. Different complexes containing TRiC/CCT and/or the chaperone prefoldin were cross-linked in absence or presence of nucleotides with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2022-12-08 | PXD030590 | Pride

A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT

Project description:Chemical cross-linking coupled to mass spectrometry was used to study assembly intermediates of the chaperonin TRiC/CCT. Complex were cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2023-08-24 | PXD043532 | Pride

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]

Project description:TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]

| PRJNA1146450 | ENA

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]

Project description:TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]

| PRJNA1146451 | ENA

TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]

Project description:TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]

| PRJNA1146452 | ENA