TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [RNA-seq]
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ABSTRACT:
PROVIDER: PRJNA1146450 | ENA |
REPOSITORIES: ENA
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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 | GSE274453 | GEO
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
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 | GSE274454 | GEO
Project description:TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [4tU-Seq]
| PRJNA1146451 | ENA
Project description:TRiC/CCT Chaperonin Regulates RNA Polymerase II in the Nucleus [DNase-Seq]
| PRJNA1146452 | ENA
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
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
Project description:The essential chaperonin TRiC/CCT mediates protein folding in cooperation with the co-chaperone prefoldin (PFD). As shown in vitro, the cylindrical TRiC complex facilitates folding through ATP-regulated client protein encapsulation. However, the functional dynamics of the chaperonin system in vivo remain unexplored. Here, we developed single-particle tracking in human cells to monitor the interactions of TRiC/PFD with newly synthesized proteins. Both chaperones engaged nascent polypeptides repeatedly in brief probing events, typically lasting around one second, with PFD recruiting TRiC. As shown with the chaperonin client actin, the co-translational interactions of PFD and TRiC increased in frequency and lifetime during chain elongation. Close to translation termination, PFD bound for several seconds, facilitating TRiC recruitment for post-translational folding involving multiple reaction cycles of ~2.5 s. Notably, the lifetimes of TRiC interactions with a folding-defective actin mutant were markedly prolonged, indicating that client conformational properties modulate TRiC function. Mutant actin continued cycling on TRiC until targeted for degradation. Surprisingly, TRiC often remained confined near its client protein between successive binding cycles, suggesting that the chaperonin machinery operates within a localized ‘protective zone’ where free diffusion is restricted. Together, these findings offer detailed insight into the single-molecule dynamics and supramolecular organization of the chaperonin system in the cellular environment.
2025-11-26 | PXD066622 | Pride
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
Project description:The eukaryotic chaperonin TRiC/CCT plays an essential role in protein folding1-4. As shown in vitro, the cylindrical TRiC complex captures unfolded client proteins and facilitates their folding through ATP-regulated encapsulation5-8. However, the functional dynamics of the chaperonin system within the cellular environment remain largely unexplored. In this study, we developed single-particle tracking in live human cells to monitor the interactions of TRiC with newly synthesized proteins, as well as its interplay with the co-chaperone PFD. We found that PFD and TRiC engage nascent protein chains in repeated, brief probing events—typically lasting around one second—with PFD acting to recruit TRiC. Using actin as an obligate chaperonin client7, the co-translational interactions of PFD and TRiC increased in both frequency and lifetime during nascent chain elongation. Near the point of translation termination, PFD interactions lasted for ~6 seconds, enabling TRiC recruitment for post-translational completion of folding via multiple reaction cycles of ~2.5 seconds. Notably, the lifetime of TRiC cycles was 3-4 times longer when a folding-defective actin mutant was analyzed, indicating that the conformational state of the client protein modulates TRiC function. Mutant actin continued cycling on TRiC until being targeted for proteasomal degradation. Unexpectedly, TRiC remained confined near its client protein between successive binding cycles, suggesting that folding occurs within a localized ‘protective zone.’ Together, these findings offer the first detailed insights into the dynamic behavior and supramolecular organization of the chaperonin system in living cells. The methodology developed in this study offers a framework for systematically investigating protein folding within the intact cellular environment.
2025-11-26 | GSE304022 | GEO