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

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

PROVIDER: PRJNA1146452 | ENA |

REPOSITORIES: ENA

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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

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

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

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

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

The TRiC Chaperonin and Prefoldin Cooperate to Fold and Assemble Viral Capsid Oligomers

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the folding of the reovirus sigma3 protein by the chaperonin, TRiC/CCT. Cross-linking was performed using the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2021-02-04 | PXD019751 | Pride

Cross-linking mass spectrometry of a complex between the chaperonin TRiC/CCT and its cochaperones, prefoldin and phosducin-like protein 2A

Project description:Chemical cross-linking coupled to mass spectrometry was used to study the architecture of the co-complex between TRiC/CCT, PFD and PhLP2A. The complex was cross-linked with the homobifunctional, noncleavable reagent, disuccinimidyl suberate (DSS).

2023-12-11 | PXD040144 | Pride

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